【著書】
1．藤田啓介 (1966).
歯学生化学（押鐘 篤 監修）. 医歯薬出版, 東京.
2．藤田啓介 (1966).
臨床病理学検査（監修 藤田啓介, 分担執筆 牛島 宥）. 藤田学園出版部, 豊明.
3．藤田啓介 (1974).
医学領域における生化学実習指針. 廣川書店, 東京.
4．藤田啓介 (1976).
医学領域における生化学(初版). 廣川書店, 東京.
5．藤田啓介 (1977).
医学領域における臨床検査学入門. フジタヘルスユニバーシティ出版会, 豊明.
6．藤田啓介 (1979).
医学領域における総合医学入門. フジタヘルスユニバーシティ出版会, 豊明.
7．藤田啓介 (1981).
医学領域における臨床看護学入門. フジタヘルスユニバーシティ出版会, 豊明.
8．藤田啓介 (1982).
医学領域における生化学実験検査指針. 廣川書店, 東京.
9．藤田啓介 (1990).
医学領域における診療放射線技術学入門. フジタヘルスユニバーシティ出版会, 豊明.
10．Fujita, K. (1993).
Aloe arborescens Miller var. natalensis Berger － The Pharmacological and Therapeutic Effects(I). Fujita Health University Press, Toyoake.
11．藤田啓介 (1994).
医学領域における生化学(改訂新版). フジタヘルスユニバーシティ出版会, 豊明.
12．藤田啓介 (1994).
キダチアロエの薬効. 現代書林, 東京.

【学術論文】

－家鶏肉種と粘液多糖類に関する研究－
1．Keisuke Fujita, Shoji Iwase. (1952).
Influence of mucin and hyaluronidase upon the growth of chicken sarcoma. Nagoya Journal of
Medical Science, 15, 261-269.
2．Keisuke Fujita, Shoji Iwase. (1953).
Influence of mucin and hyaluronidase upon the growth of chicken sarcoma. With special regard
to the histological observation. Nagoya Journal of Medical Science, 16, 298-305.
3．藤田啓介 (1953).
家鶏肉腫粘液多糖類の生物学上の意義について. 現代医学, 3, 162-163.
4. Keisuke Fujita. (1954).
The metabolic pattern of chicken sarcoma. Nagoya Journal of Medical Science, 17, 30-36.
5. Keisuke Fujita. (1954).
The chemical properties of a polysaccharide in chicken sarcoma. Nagoya Journal of Medical
Science, 17, 98-101.

－トリパンブルーの肝発がん作用に関する研究－
1. Shoji Iwase. Keisuke Fujita. (1953).
Hepatoma inhibition in rats fed DAB by the injection of trypan blue. Nagoya Journal of Medical
Science, 16, 307-310.
2. S. Iwase, K. Fujita. (1955).
Inhibiting effect of trypan blue on the experimental production of liver cancer. Nature, 175, 552.
3. Keisuke Fujita, Shoji Iwase, Toshio Matsubara, Isao Ishiguro, Hiroshi Matsui, TetsuhikoMizuno, Toyohisa Arai, Tetsuya Takayanagi, Yasuyo Sugiyama, Kyoko Shirafuji. (1956).
Biochemical interaction of trypan blue and p-dimethylaminoazobenzene in the liver of rat (1).
Gann, 47, 181-206.
4. K. Fujita, T. Mine, S. Iwase, T. Mizuno, T. Takayanagi, Y. Sugiyama, T. Arai. (1957).
The carcinogenicity of certain compounds related to trypan blue. British Journal of Experimental
Pathology, 38, 291-296.
5. Shoji Iwase, Keisuke Fujita. (1957).

Effect of trypan red and methyl orange on the experimental production of liver cancer. Nagoya
Journal of Medical Science, 19, 189-192.
6. Keisuke Fujita, Shoji Iwase, Tetsuhiko Ito, Toyohisa Arai, Tetsuya Takayanagi, Yasuyo
Sugiyama, Mutsushi Matsuyama, Chie Takagi, Takeyo Ohmae, Takao Mine. (1957).
Biochemical interaction of trypan blue and D-dimethylaminoazobenzene in the liver of rat (II):The inhibitory effect of trypan blue on the experimental production of liver carcinoma. Gann, 48,
277-288.
7. K. Fujita, S. Iwase, T. Ito, M. Matsuyama. (1958).
Inhibiting effect of chlorpromazine on the experimental production of liver cancer. Nature, 181,
54.
8. K. Fujita, T. Mine, T. Ito, M. Matsuyama. (1958).
Effects of certain compounds related to trypan blue on the experimental production of livercancer. Nature, 181, 1732-1733.
9. 藤田啓介 (1960).
発癌物質－その溶解性と発癌性について. 現代医学, 7, 137-140.

－アロエの薬理作用に関する研究－
1. Fujita, K., Teradaira, R., and Nagatsu, T. (1976).
Bradykininase activity of aloe extract. Biochem. Pharmacol., 25, 205.
2. Fujita, K., Yamada, Y., Azuma, K., and Hirosawa, S. (1978).
Effect of leaf extracts of Aloe arborescens Mill, subsp. natalensis Berger on growth of
Trichophyton mentagrophytes. Antimicrob. Agents Chemother., 14, 132-136.
3. Fujita, K., Suzuki, I., Ochiai, J. Shinpo, K., Inoue, S., and Saito, H. (1978).
Specific reaction of aloe extract with serum proteins of various animals. Experientia, 34, 523-524.
4. Fujita, K., Ito, S., Teradaira, R., and Beppu, H. (1979).
Properties of a carboxypeptidase from aloe. Biochem. Pharmacol., 28, 1261-1262.
5. 別府秀彦, 川井 薫, 千原

猛, 新保 寛, 藤田啓介 (1990).

自然発症糖尿病ハツカネズミに対するキダチアロエの血糖降下作用. 医学と生物学, 120,151-156.

6. 川井 薫, 津田洋幸, 千原

猛, 別府秀彦, 新保

寛, 永津俊治, 廣野

巖, 藤田啓介(1992).
ラット肝前癌病変の増殖過程におけるキダチアロエの抑制効果と赤血球および肝組織ポリ
アミン･レベル. 医学と生物学, 125, 189-194.
7. 川井

薫, 津田洋幸, 千原

猛, 別府秀彦, 新保 寛, 永津俊治, 廣野 巖, 藤田啓介

(1992).
ラット肝発癌イニシエーション作用に対するキダチアロエの抑制効果と赤血球および肝組
織ポリアミン･レベル. 医学と生物学, 125, 195-200.
8. Kawai, K., Beppu, H., Koike, T., Fujita, K., and Marunouchi, T. (1993).
Tissue culture of Aloe arborescens Miller var. natalensis Berger. Phytother. Res., 7, S5-S10.
9. Ito, S., Teradaira, R., Beppu, H., Obata, M., Fujita, K., and Nagatsu, T. (1993).
Biochemical properties of carboxypeptidase from Aloe arborescens Miller var. natalensis Berger.
Phytother. Res., 7, S26-S29.
10. Obata, M., Ito, S., Beppu, H., Fujita, K., and Nagatsu, T. (1993).
Mechanism of antiinflammatory and antithermal burn action of CPase from Aloe arborescens
Miller var. natalensis Berger in rats and mice. Phytother. Res., 7, S30-S33.
11. Teradaira,R., Shinzato, M., Beppu, H., and Fujita, K. (1993).
Antigastric ulcer effects in Rats of Aloe arborescens Miller var. natalensis Berger extract.
Phytother. Res., 7, S34-S36.
12. Beppu, H., Nagamura, Y., and Fujita, K. (1993).
Hypoglycaemia and antidiabetic effects in mice of Aloe arborescens Miller var. natalensis Berger.
Phytother. Res., 7, S37-S42.
13. Tsuda, H., Matsumoto, K., Ito, M., Hirano, I., Kawai, K., Beppu, H., Fujita, K., and Nagao,
M. (1993).
Inhibitory effect of Aloe arboresens Miller var. natalensis Berger (Kidachi aloe) on induction ofpreneoplastic focal lesions in the rat liver. Phytother. Res., 7, S43-S47.
14. Koike, T., Beppu, H., Kuzuya, H., Maruta, K., Shimpo, K., Suzuki, M., Titani, K., and Fujita,
K. (1995).
A 35 kDa mannose-binding lectin with hemagglutinating and mitogenic activities from "Kidachi
Aloe" (Aloe arborescens Miller var. natalensis Berger). Journal of Biochemistry, 118, 1205-1210.
15. Koike, T., Titani, K., Suzuki, M., Beppu, H., Kuzuya, H., Maruta, K., Shimpo, K., and Fujita,K. (1995).
The complete amino acid sequence of a mannose-binding lectin from "Kidachi Aloe" (Aloearborescens Miller var. natalensis Berger). Biochemical and Biophysical ResearchCommunications, 214, 163-170.
16. Uehara, N., Iwahori, Y., Asamoto, M., Baba-Toriyama, H., Iigo, M., Ochiai, M., Nagao, M.,
Nakayama, M., Degawa, M., Matsumoto, K., Hirono, I., Beppu, H., Fujita, K., and Tsuda, H.
(1996).
Decreased levels of 2-amino-3-methylimidazo[4,5-f]quinoline-DNA adducts in rats treated with
β-carotene, α-tocopherol and freeze-dried Aloe. Japanese Journal of Cancer Research, 87,
342-348.

－がんの生化学的指標としてのポリアミンの定量とその意義－
1. Fujita, K., Nagatsu, T., Maruta, K., Ito, M., Senba, H., and Miki, K. (1976).
Urinary putrescine, spermidine, and spermine in human blood and solid cancers and in anexperimental gastric tumor of rats. Cancer Res., 36, 1320-1324.
2. 藤田啓介, 伊藤 圓, 丸田一裕, 嶋田芳子, 新美 元, 坂本芳子 (1977).
癌患者における尿中の Putrescine 対 Ornithine 比について. 藤田学園医学会誌, 1, 115-118.
3.

藤田啓介, 伊藤 圓, 大谷元彦, 大田みどり, 丸田一裕, 坂本芳子 (1977).

小児腎疾患における尿中の Polyamine 量と各種臨床検査成績との関連について.

藤田学園

医学会誌, 1, 119-123.
4. Fujita, K., Nagatsu, T., Shinpo, K., Maruta, K., Takahashi, H., and Sekiya, A. (1978).
Increase of urinary putrescine in 3,4-benzopyrene carcinogenesis and its inhibition by putrescine.
Cancer Res., 38, 3509-3511.
5. Fujita, K., Nagatsu, T., Shinpo, K., Maruta, K., Teradaira, R., and Nakamura, M. (1980).
Improved analysis for urinary polyamines by use of high voltage electrophoresis on paper. Clin.
Chem., 26, 1577-1582.
6. 寺平良治, 藤田啓介, 関谷
14

淳, 鹿島正俊 (1981).

C-Putrescine のマウスにおける吸収, 分布, 排泄. Radioisotopes, 30, 140-145.

7. 藤田啓介, 永津俊治, 新保

寛 (1981).

ポリアミン定量法. 蛋白質 核酸 酵素, 26, 1273-1288.

8. 藤田啓介, 永津俊治, 新保

寛 (1981).

ポリアミンとがん. 蛋白質 核酸 酵素, 26, 1884-1894.
9. Shinpo, K., Fujita, K., Maruta, K., Teradaira, R., and Nagatsu, T. (1983).
Comparative measurements of urinary polyamines in early morning and 24-hour urine specimens.
Clin. Chim. Acta, 131, 143-148.
10. Fujita, K., Nagatsu, T., and Shinpo, K. (1983).
Assay methods for polyamines. In: Methods in Biogenic Amine Reseach. Parvez, S., Nagatsu, T.,
Nagatsu, I., Parvez, H. (Eds.). Elsevier, Amsterdam, pp. 741-776.
11. 寺平良治, 藤田啓介, 高橋久英 (1983).
Putrescine のラットにおける急性毒性試験. 応用薬理, 25, 489-499.
12. Nagatsu, T., Yamaguchi, T., Sawada, M., Fujita, K., Shinpo, K., Ito, M., Hirano, M.,
Sugimoto, T., Matsuura, S., and Akino, M. (1984).
Elevated levels of polyamines and radioimmunoassayable 6-hydroxymethylpterin-like compoundin urine from cancer patients. Biogenic Amines, 1, 51-62.
13. 永津俊治, 松井俊和, 新保

寛, 藤田啓介 (1984).

ポリアミン生体内動態と代謝. 臨床病理, 59, 23-28.
14. 新保寛, 川井 薫, 松井俊和, 中村康一, 北川康雄, 新里昌功, 伊藤祥輔, 平野正美, 伊藤圓, 永津俊治, 藤田啓介 (1984).
悪性腫瘍患者の尿中アセチルポリアミン. 臨床病理, 59, 29-37.
15. 新保正美, 伊藤寛, 川井 薫, 小川 忠, 松井俊和, 清水鈴昭, 北川康雄, 柳生 茂, 高橋久英, 平野圓, 永津俊治, 藤田啓介 (1984).

赤血球ポリアミンの測定法と臨床応用. 臨床病理, 59, 157-166.
16. Nagatsu, T., Shimpo, K., Kawai, K., Shinzato, M., Ito, S., Matsui, T., Nakamura, K.,
Kitagawa, Y., Hirano, M., Ito, M., and Fujita, K. (1985).
Acetylpolyamines in urine and polyamines in erythrocytes as biochemical markers of cancer. In:
Polyamines; Basic and Clinical Aspects. Imahori, K., Suzuki, F., Suzuki, O., Bachrach, U. (Eds.).
VNU Science Press, Utrecht, The Netherlands, pp. 349-356.
17. Watanabe, N., Asano, M., Yamamoto, K., Nagatsu, T., Matsumoto, T., and Fujita, K. (1988).
Electrochemical detection of polyamines using immobilized enzyme as postcolumn reactor inhigh performance liquid chromatography. Chemistry Lett., 1169-1170.

18. Maruta, K., Teradaira, R., Watanabe, N., Nagatsu, T., Asano, M, Yamamoto, K., Matsumoto,T., Shionoya, Y., and Fujita, K. (1989).
Simple, sensitive assay of polyamines by high-performance liquid chromatography withelectrochemical detection after post-column reaction with immobilized polyamine oxidase. Clin.
Chem., 35, 1694-1696.
19. Watanabe, N., Asano, M., Yamamoto, K., Nagatsu, T., Matsumoto, T., and Fujita, K. (1989).
High performance liquid chromatography of biological polyamines using immobilized enzyme as
post-column reactor followed by electrochemical detection. Biomed. Chromatogr., 3, 187-191.
20. Hibino, T., Shimpo, K., Kawai, K., Chihara, T., Maruta, K., Arai, M., Nagatsu, T., and Fujita,
K. (1990).
Polyamine levels of urine and erythrocytes on inhibition of DMBA-induced oral carcinogenesis
by topical beta-carotene. Biogenic Amines, 7, 209-216.
21. 新保寛, 川井 薫, 丸田一皓, 寺平 竜, 永津俊治, 藤田啓介 (1990).

尿中ポリアミン測定. Medical Technology, 18(9), 855-861.
22. Ogiwara, S., Nagatsu, T., Teradaira, R., Fujita K., and Sugimoto, T. (1992).
Occurrence of umanopterin, a new diastereomer of neopterin, in urine from cancer patients.
Tetrahedron Lett., 33, 1341-1342.
23. Sugimoto, T., Ogiwara, S., Teradaira, R., Fujita, K., and Nagatsu, T. (1992).
Determination of oncopterin isolated from urine of cancer patients as N2-(3-aminopropyl)
biopterin. Biogenic Amines, 9, 77-82.
24. Ogiwara, S., Hidaka, H., Sugimoto, T., Teradaira, R., Fujita, K., and Nagatsu, T. (1993).
Elevated levels of oncopterin, N2-(3-aminopropyl) biopterin, a new pterin compound, in urine
from patients with solid and blood cancers. J. Biochem., 113, 1-3.
25. Fujita, K., Nagatsu, T., and Shimpo, K. (1993).
Assay methods for polyamines. In: Methods in Neurotransmitter and Neuropeptide Research.
Parvez, S.H., Naoi, M., Nagatsu, T., Parvez, S. (Eds.). Elsevier Science Publishers B.V.,
Amsterdam, pp. 189-228.

－ビタミン関連物質の抗腫瘍効果ならびに制がん剤副作用の軽減－
1. Fujita, K., Shinpo, K., Yamada, K., Sato, T., Niimi, H., Shamoto, M., Nagatsu, T., Takeuchi,
T. and Umezawa, H. (1982).

Reduction of adriamycin toxicity by ascorbate in mice and guinea pigs. Cancer Res., 42, 309-316.
2. Shimpo, K., Nagatsu, T., Yamada, K., Sato, T., Niimi, H., Shamoto, M., Takeuchi. T.,
Umezawa, H., and Fujita, K. (1991).
Ascorbic acid and adriamycin toxicity. Am. J. Clin. Neutr., 54, 1298S-1301S.

－メラニン前駆体による悪性黒色腫の診断と治療－
1. Ito, S., Teradaira, R., and Fujita, K. (1980).
Distribution and metabolism of tritium-labelled 5-S-cysteinyldopa in mice. Biochem. Pharmacol.,29, 3277-3280.
2. Fujita, K., Ito, S., Inoue, S., Yamamoto, Y., Takeuchi, J., Shamoto, M., and Nagatsu, T.
(1980).
Selective toxicity of 5-S-cysteinyldopa, a melanin precursor, to tumor cells in vitro and in vivo.
Cancer Res., 40, 2543-2546.
3. Ito. S., and Fujita, K. (1981).
Formation of cysteine conjugates from dihydroxyphenylalanine and its S-cysteinyl derivatives by
peroxidase-catalyzed oxidation. Biochim. Biophys. Acta, 672, 151-157.
4. Ito, S., Inoue, S., Yamamoto, Y., and Fujita, K. (1981).
Synthesis and antitumor activity of cysteinyl-3,4-dihydroxyphenylalanines and related compounds.
J. Med. Chem., 24, 673-677.
5. Ito, S., and Fujita, K. (1981).
New possible routes for the biosynthesis of cysteinyldopas and related metabolites. In: Pigment
Cell 1981. Phenotypic Expression in Pigment Cells. Seiji, M. (Ed.). University of Tokyo Press,
1981, pp. 85-91.
6. Ito, S., and Fujita, K. (1982).
Conjugation of dopa and 5-S-cysteinyldopa with cysteine mediated by superoxide radical.
Biochem. Pharmacol., 31, 2887-2889.
7. Ito, S., Inoue, S., and Fujita, K. (1983).
The mechanism of toxicity of 5-S-cysteinyldopa to tumour cells. Hydrogen peroxide as amediator of cytotoxicity. Biochem. Pharmacol., 32, 2079-2081.
8. Ito, S., Homma, K., Kiyota, M., Fujita, K., and Jimbow, K. (1983)

Characterization of structural properties for morphologic differentiation of melanosomes. Ⅲ. Freeand protein-bound dopa and 5-S-cysteinyldopa in B16 and Harding-Passey melanomas. J. Invest.
Dermatol., 80, 207-209.
9. Ito, S., Jimbow, K., Kato, T., Kiyota, M., and Fujita, K. (1983).
Protein-bound dopa and 5-S-cysteinyldopa in non-melanogenic tissues. Acta Derm. Venereol.
(Stockh.), 63, 463-467.
10. Ito, S., and Fujita, K. (1984).
Oxygen-dependent conjugation of dopa with cysteine catalysed by iron-EDTA complex. Biochem.
Pharmacol., 33, 2193-2197.
11. Ito, S., Fujita, K., Takahashi, H., and Jinbow, K. (1984).
Characterization of melanogenesis in mouse and guinea pig hair by chemical analysis of melaninsand of free and bound dopa and 5-S-cysteinyldopa. J. Invest. Dermatol., 83, 12-14.
12. Ito, S., Kato, T., Maruta, K., and Fujita, K. (1984).
Determination of DOPA, dopamine, and 5-S-cysteinyl-DOPA in plasma, urine, and tissue samples
by high-performance liquid chromatography with electrochemical detection. J. Chromatogr., 311,
154-159.
13. Ito, S., Kato, T., Shinpo, K., and Fujita, K. (1984).
Oxidation of tyrosine residues in proteins by tyrosinase. Formation of Protein-bonded
3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine. Biochem. J., 222,
407-411.
14. Ito, S., and Fujita, K. (1985).
Microanalysis of eumelanin and pheomelanin in hair and melanomas by chemical degradationand liquid chromatography. Anal. Biochem., 144, 527-536.
15. Ito, S., Kato, T., Maruta, K., Kurahashi, T., and Fujita, K. (1985).
Determination of DOPA, dopamine, and 5-S-cysteinyldopa in plasma, urine, and tissue samples
by high-performance liquid chromatography with electrochemical detection. Proc. Jpn. Soc. Invest.
Dermatol., 9, 13-14.
16. Kato, T., Ito, S., and Fujita, K. (1986).
Tyrosinase-catalyzed binding of 3,4-dihydroxyphenylalanine with proteins through the sulfhydryl
group. Biochim. Biophys. Acta, 881, 415-421.
17. Ito, Y., Jimbow, K., and Ito, S. (1986).

Depigmentation of black guinea pig skin by topical application of cysteaminylphenol,
cysteinylphenol, and related compounds. J. Invest. Dermatol., 88, 77-82.
18. Ito, S., Fujita, K., Kato, T., Shinpo, K., Takahashi, H., and Jimbow, K. (1986).
Occurrence and Biosynthesis of Protein-Bound Dopa and Cysteinyldopas. In: Structure andFunction of Melanin. Jimbow, K. (Ed.). Fuji shoin, Sapporo, pp. 31-43.
19. Inoue, S., Ito, S., Imai, Y., Kasuga, T., and Fujita, K. (1987).
Growth inhibition of melanoma cells by N-protected dopa derivatives. Biochem. Pharmacol., 36,3537-3540.
20. Ito, S., Kato, T., and Fujita, K. (1987).
Seasonal variation in urinary excretion of 5-S-cysteinyldopa in healthy Japanese. Acta Derm.
Venereol. (Stockh.), 67, 163-165.
21. Miura, S., Ueda, T., Jimbow, K., Ito, S., and Fujita, K. (1987).
Synthesis of cysteinylphenol, cysteaminylphenol, and related compounds, and in vivo evaluationof antimelanoma effect. Arch. Dermatol. Res., 279,
219-225.
22. 井上茂樹, 伊藤祥輔, 藤田啓介 (1987).
N-アセチルドーパエチルエステルによるメラノーマ細胞の増殖抑制. 藤田学園医学会誌, 11,285-288.
23. Naoi, M., Takahashi, T., Ito, S., Fujita, K., and Nagatsu, T. (1988).
Accumulation of N-methyl-4-phenylpyridinium ion (MPP+) in human melanoma cell line, HMVI and - II. Neurosci. Lett., 87, 57-62.
24. Ito, S., Imai, Y., Jimbow, K., and Fujita, K. (1988).
Incorporation of sulfhydryl compounds into melanins in vitro. Biochim. Biophys. Acta, 964, 1-7.
25.

Wakamatsu, K., Ito, S., and Fujita, K. (1988).

Melanin-related metabolites in urine of B16 melanoma-bearing mice. Acta Derm. Venereol.
(Stockh.), 68, 385-389.
26. Ito, S., Kato, T., and Fujita, K. (1988).
Covalent binding of catechols to proteins through the sulphydryl group. Biochem. Pharmacol., 37,
1707-1710.
27. Ito, S., Wakamatsu, K., Inoue, S., and Fujita, K. (1989).

Correlation between urinary melanin-related metabolites and tumour weight in melanoma-bearing
mice. Acta Derm. Venereol. (Stockh.), 69, 380-384.
28. Inoue, S., Ito, S., Wakamatsu, K., Jimbow, K., and Fujita, K. (1990).
Mechanism of growth inhibition of melanoma cells by 4-S-cysteaminylphenol and its analogues.
Biochem. Pharmacol., 39, 1077-1083.
29. Wakamatsu, K., Ito, S., and Fujita, K. (1990).
Production, circulation, and excretion of melanin-related metabolites in B16 melanoma-bearing
mice. Acta Derm. Venereol. (Stockh.), 70, 367-372.
30. 長谷川勝俊, 井上茂樹, 伊藤祥輔, 若松一雅, 藤田啓介 (1992).
メラニン親和性を有する 4-S-システアミニルフェノールによる黒色腫細胞に対する選択的毒性. 藤田学園医学会誌, 16, 43-47.
31. Hasegawa, K., Inoue, S., Wakamatsu, K., Ito, S., Fujita, K., and Ishikawa, K. (1993).
Changes in plasma 5-S-cysteinyldopa concentration in B16 melanoma-bearing mice treated withinterferon-β or dacarbazine. Melanoma Res., 3, 377-380.
32. Inoue, S., Hasegawa, K., Ito, S., Wakamatsu, K., and Fujita, K. (1993).
Antimelanoma activity of chloroquine, an antimalarial agent with high affinity for melanin.
Pigment Cell Res., 6, 354-358.

－精神分裂病の生化学指標としてのドーパミンβ-水酸化酵素の定量とその意義－
1. Fujita, K., Nagatsu, T., Maruta, K., Teradaira, R., Beppu, H., Tsuji, Y., and Kato, T. (1977).
Fluorescence assays for dopamine β-hydroxylase activity in human serum by high-performanceliquid chromatography. Anal. Biochem., 82, 130-140.
2. Fujita, K., Maruta, K., Teradaira, R., Beppu, H., Ikegame, M., Nagatsu, T., and Kato, T.
(1977).
Normal values for serum dopamine β-hydroxylase activity. Clin. Chem., 23, 1947.
3. Fujita, K., Maruta, K., Teradaira, R., Beppu, H., Shinpo, K., Maeno, Y., Ito, T., Nagatsu, T.,
and Kato, T. (1977).
Dopamine β-hydroxylase activity in human cerebrospinal fluid and serum. J. Neurochem., 29,1141-1142.
4. Fujita, K., Ito, T., Maruta, K., Teradaira, R., Beppu, H., Nakagami, Y., Kato, Y., Nagatsu, T.,and Kato, T. (1978).
Serum dopamine β-hydroxylase in schizophrenic patients. J. Neurochem., 30, 1569-1572.
5. Fujita, K., Ito, T., Maruta, K., Teradaira, R., Beppu, H., Nakagami, Y., Kato,Y., Nagatsu, T.,
and Kato, T. (1979)
Serum dopamine β-hydroxylase in schizophrenic patients. In: Catecholamines: Basic andClinical Frontiers. Volume Two. Usdin, E., Kopin, I.J. Barchas, J. (Eds.). Pergamon Press, New
York, pp. 1940-1942.
6. Nagatsu, T., Kato, T., Fujita, K., Takahashi, H., Inoue, T., Teradaira, R., Beppu, H., Kawai,K., Maruta, K., Yagyu, S., and Sato, T. (1980).
Catecholamine synthesizing enzymes of spontaneously hypertensive rats under stress. In:
Catecholamines and Stress: Recent Advances. Usdin, E., Kvetnansky, R., Kopin, I.J. (Eds.).
Elsevier, North-Holland, pp. 339-348.
7. Matsui, H., Kato, T., Yamamoto, C., Fujita, K., and Nagatsu, T. (1981).
Highly sensitive assay for dopamine β-hydroxylase activity in human cerebrospinal fluid by highperformance liquid chromatography-electrochemical detection: Properties of the enzyme. J.
Neurochem., 37, 289-296.
8. Fujita, K., Teradaira, R., Inoue, T., Takahashi, H., Yagyu, S., and Nagatsu, T. (1982).
In vivo and in vitro dopamine β-hydroxylase activity in spontaneously hypertensive rats:
Changes by stress. In: Hypertensive Mechanisms. The Spontaneously Hypertensive Rat as a
Model to Study Human Hypertension. Rascher, W., Clough, D., Ganten, D. (Eds.). F. K.
Schattauer Verlag, Stuttgart, pp. 481-484.
9. Nagatsu, T., Wakui, Y., Kato, T., Fujita, K., Kondo, T., Yokochi, F., and Narabayashi, H.
(1982).
Dopamine β-hydroxylase activity in cerebrospinal fluid of Parkinsonian patients. Biomed. Res.,3, 95-98.
10. Fujita, K., Maruta, K., Teradaira, R., Beppu, H., Ikegame, M., Kawai, K., and Nagatsu, T.
(1982).
Dopamine β-hydroxylase activity in human cerebrospinal fluid from various age groups. Clin.
Chem., 28, 1403-1404.
11. Fujita, K., Teradaira, R., Inoue, T., Takahashi, H., Beppu, H., Kawai, K., Maruta, K. Yagyu,
S., and Nagatsu, T. (1982).
Stress-induced changes in in vivo and in vitro dopamine β-hydroxylase activity in spontaneously
hypertensive rats. Biochem. Med., 28, 340-346.

12. Kawai, K., Maruta, K., Nagatsu, T., Teradaira, R., Matsui, H., Ito, I., Ohtani, M., Shinohara,Y., and Fujita, K. (1992).
The circadian variation of the serum dopamine β-hydroxylase activity as a biochemical marker
in schizophrenia. Biogenic Amines, 9(2), 83-98.

－カテコールアミンに関する研究－
1. 永津俊治, 加藤 武, 楢林博太郎, 飯塚礼二, 藤田啓介 (1980).
パーキンソン病患者脳脊髄液のドーパミンβ-水酸化酵素活性. 厚生省特定研究変性性神経疾患調査研究班 1979 年報告書, 262-265.
2. Oka, K., Sekiya, M., Osada, H., Fujita, K., Kato, T., and Nagatsu, T. (1982).
Simultaneous fluorometry of urinary dopamine, norepinephrine, and epinephrine compared withliquid chromatography with electrochemical detection. Clin. Chem., 28, 646-649.
3. Matsui, H., Kato, N., Yamamoto, C., Fujita, K., Sakai, H., and Nagatsu, T. (1984).
A sensitive fluorometric assay for dopamine β-hydroxylase activity by high-performance liquid
chromatography. Biochem. Med., 31, 140-146.
4. Ikeda, M., Hirata, Y., Fujita, K., Shinzato, M., Takahashi, H., Yagyu, S., and Nagatsu, T.
(1984).
Effects of stress on release of dopamine and serotonin in the striatum of spontaneously
hypertensive rats: An In vivo voltammetric study. Neurochem. Int., 6, 509-512.
5. 永津俊治, 藤田啓介, 川井薫, 新保 寛, 新里昌功 (1984).

精神分裂病. 日本臨牀, 42, 891-901.
6. Nagatsu, T., Ikeda, M., Hirata, Y., Fujita, K., Takahashi, H., Shinzato, M., and Yagyu, S.
(1984).
Abnormality in catecholamine metabolism in the brain of spontaneously hypertensive rats (SHR)-analysis by In vivo voltammetry. Jpn. Heart J., 25, 820-822.
7. 永津俊治, 高橋久英, 池田正人, 柳生 茂, 新里昌功, 藤田啓介 (1984).
SHR を用いた病態代謝研究法－ In vivo voltammetry を中心に. 代謝, 21, 1135-1144.
8. Nagatsu, T., Ikeda, M., Inagaki, H., Rahman, M.K., Fujita, K., Takahashi, H., Shinzato, M.,
and Yagyu, S. (1984).
Effect of stress on central monoaminergic neurons as measured by in vivo voltammetry and on

serum aromatic L-amino acid decarboxylase activity of spontaneously hypertensive rats. In:
Stress: The Role of Catecholamines and Other Neurotransmitters. Usdin, E., Kvetnansky, R.,
Axelrod, J. (Eds.). Gordon and Breach Science Publishers, New York, pp. 425-433.
9. Nagatsu, I., Ito, M., Kawakami, Y., Karasawa, N., Takahashi, H., Fujita, K., and Nagatsu, T.
(1985).
Quantitative immunofluorescence of tyrosine hydroxylase in the adrenal medulla of spontaneously
hypertensive rats. Experientia, 41, 1054-1055.
10. Togari, A., Murakami, T., Oshima, T., Fujita, K., and Nagatsu, T. (1986).
Effects of polyamines on tyrosine hydroxylase activity in adrenals. Neurochem. Int., 9, 281-286.
11. Nagatsu, T., Hirata, Y., Sawada, M., Ikeda, M., Adachi, T., Shinohara, Y., Takahashi, H.,
Yagi, S., and Fujita, K. (1986).
Abnormality of central monoaminergic neurons in spontaneously hypertension rats: in vitro andIn vivo (voltammetry) studies. In: Brain and Blood Pressure Control. Nakamura, K. (Ed.).
Elsevier Science Publishers B.V., Amsterdam, pp. 337-341.
12. Kaneda, N., Kobayashi, K., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K.,
and Nagatsu, T. (1987).
Isolation of a novel cDNA clone for human tyrosine hydroxylase alternative RNA splicing
produces four kinds of mRNA from a single gene. Biochem. Biophys. Res. Commun., 146,
971-975.
13. Kobayashi, K., Kaneda, N., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K.,
and Nagatsu, T. (1987).
Isolation of a full length cDNA clone encoding human tyrosine hydroxylase type 3. Nucleic
Acids Res., 15, 6733.
14. Mogi, M., Harada, M., Kojima, K., Inagaki, H., Kondo, T., Narabayashi, H., Arai, T.,
Teradaira, R., Fujita, K., Kiuchi, K., and Nagatsu, T. (1988).
Sandwich enzyme immunoassay of dopamine β-hydroxylase in cerebrospinal fluid from control
and parkinsonian patients. Neurochem. Int., 12, 187-191.
15. Kobayashi, K., Kaneda, N., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K.,
and Nagatsu, T. (1988).
Structure of the human tyrosine hydroxylase gene: Alternative splicing from a single geneaccounts for generation of four mRNA types. J. Biochem., 103, 907-912.
16. Kaneda, N., Ichinose, H., Kobayashi, K., Oka, K., Kishi, F., Nakazawa, A., Kurosawa, Y.,Fujita, K., and Nagatsu, T. (1988).
Molecular cloning of cDNA and chromosomal assignment of the gene for human
phenylethanolamine N-methyltransferase, the enzyme for epinephrine biosynthesis. J. Biol. Chem.,
263, 7672-7677
17. Kobayashi, K., Kiuchi, K., Ishii, A., Kaneda, N., Kurosawa, Y., Fujita, K., and Nagatsu, T.
(1988).
Expression of four types of human tyrosine hydroxylase in COS cells. FEBS Lett., 238, 431-434.
18. Uchida, K., Takamatsu, K., Kaneda, N., Toya, S., Tsukada, Y., Kurosawa, Y., Fujita, K.,
Nagatsu, T., and Kohsaka, S. (1988).
Transfection of tyrosine hydroxylase cDNA into C6 cells: the synthesis and release of L-DOPA.
Proc. Japan Acad., 64, 290-293.
19. Nagatsu, T., Ikeda, M., Adachi, T., Shinohara, Y., Shinzato, M., Takahashi, H., and Fujita, K.
(1988).
Abnormal catecholamine metabolism in spontaneously hypertensive rats voltammetry in vivo. In:
Progress in Hypertension, Vol. 1. Saito, H. (Ed.). VNU Science Press, Utrecht, pp. 1-8.
20. Kobayashi, K., Kurosawa, Y., Fujita, K., and Nagatsu, T. (1989).
Human dopamine β-hydroxylase gene: two mRNA types having different 3'-terminal regions areproduced through alternative polyadenylation. Nucleic Acid Res., 17, 1089-1102.
21. Uchida, K., Takamatsu, K., Kaneda, N., Toya, S., Tsukada, Y., Kurosawa, Y., Fujita, K.,
Nagatsu, T., and Kohsaka, S. (1989).
Synthesis of L-3,4-dihydroxyphenylalanine by tyrosine hydroxylase cDNA-transfected C6 cells:
application for intracerebral grafting. J. Neurochem., 53, 728-732.
22. Ichinose, H., Kurosawa, Y., Titani, K., Fujita, K., and Nagatsu, T. (1989).
Isolation and characterization of a cDNA clone encoding human aromatic L-amino aciddecarboxylase. Biochem. Biophys. Res. Commun., 164, 1024-1030.
23. Sasaoka, T., Kaneda, N., Kurosawa, Y., Fujita, K., and Nagatsu, T. (1989).
Structure of human phenylethanolamine N-methyltransferase gene:existence of two types ofmRNA with different transcription initiation sites. Neurochem. Int., 15, 555-565.
24. Nagatsu, T., Kaneda, N., Kobayashi, K., Ichinose, H., Sasaoka, T., Ishii, A., Kiuchi, K.,
Kurosawa, Y., and Fujita, K. (1989).
Molecular genetic approaches to the study of human catecholamine-synthesizing enzymes. In:
Bioinformatics. Hatase, O., Wang, J.H. (Eds.). Elsevier Science Publishers B. V., Amsterdam, pp.

281-288.
25. Nagatsu, T., Ino, K., Majima, Y., Beppu, H., Fujioka, K., Iwase, S., Suzuki, S., Chihara, T.,
and Fujita, K. (1989).
Changes of brain monoamines under stress measured in vivo by voltammetry. In: Stress:
Neurochemical and Humoral Mechanisms. G. R. Van Loon, Kvetnansky, R., McCarry, R.,
Axelrod, J. (Eds.). Gordon and Breach Science, New York, pp. 43-51.
26. Nagatsu, I., Kobayashi, K., Fujii, T., Komori, K., Sekiguchi, K., Titani, K., Fujita, K., andNagatsu, T.(1990).
Antibodies raised against different oligopeptide segments of human dopamine β-hydroxylase.
Neurosci. Lett., 120, 141-145.
27. Kaneda, N., Kobayashi, K., Ichinose, H., Sasaoka, T., Ishii, A., Kiuchi, K., Kurosawa, Y.,
Fujita, K., and Nagatsu, T. (1990).
Molecular biological approaches to catecholamine neurotransmitters and brain aging. In: Aging of
the Brain: Cellular and Molecular Aspects of Brain Aging and Alzheimer's Disease. Nagatsu, T.,
Hayaishi, O. (Eds.). Japan Scientific Societies Press, Tokyo and Karger, Basel, pp. 53-66.
28. Nagatsu, T., Kaneda, N., Kobayashi, K., Ichinose H., Sasaoka, T., Ishii, A., Kiuchi, K., Fujita,
K., Titani, K., and Kurosawa, Y. (1990).
Genes of human catecholamine-synthesizing enzymes. In: Basic, Clinical, and Therapeutic
Aspects of Alzheimer's and Parkinson's Diseases, Vol. 1. T. Nagatsu, A. Fisher, and M. Yoshida(Eds.). Plenum Press, New York, pp. 481-486.
29. Kiuchi, K., Kiuchi, K., Titani, K., Fujita, K., Suzuki, K., and Nagatsu, T. (1991).
Limited proteolysis of tyrosine hydroxylase by Ca2+-activated neutral protease (Calpain).
Biochemistry, 30, 10416-10419.
30. Ichinose, H., Katoh, S., Sueoka, T., Titani, K., Fujita, K., and Nagatsu, T. (1991).
Cloning and sequencing of cDNA encoding human sepiapterin reductase. － An Enzyme involvedin tetrahydrobiopterin biosynthesis － Biochem. Biophys. Res. Commun., 179, 183-189.
31. Yamada, K., Sakai, M., Takeuchi, T., Karasawa, N., Kaneda, N., Sasaoka, T., Kobayashi, K.,
Yokoyama, M., Nomura, T., Katsuki, M., Fujita, K., Nagatsu, T., and Nagatsu, I. (1991).
Enhanced expression of human tyrosine hydroxylase in the lower brainstem of transgenic mice.
Neurosci. Lett., 134(1), 57-61.
32. Kaneda, N., Sasaoka, T., Kobayashi, K., Kiuchi, K., Nagatsu, I., Kurosawa, Y., Fujita. K.,
Yokoyama, M., Nomura, T., Katsuki, M., and Nagatsu, T. (1991).

Tissue-specific and high-level expression of the human tyrosine hydroxylase gene in transgenic
mice. Neuron, 6, 583-594.
33. Nagatsu, I., Yamada, K., Karasawa, N., Sasaoka, T., Kobayashi, K.,Yokoyama, M., Nomura,T., Katsuki, M., Fujita, K., and Nagatsu, T. (1991).
Expression in brain sensory neurons of the transgene in transgenic mice carrying human tyrosinehydroxylase gene. Neurosci. Lett., 127, 91-95.
34. Ichinose, H., Sumi, C., Kurosawa, Y., Titani, K., Fujita, K., and Nagatsu, T. (1991).
Isolation and characterization of a cDNA clone encoding human aromatic L-amino aciddecarboxylase. In: Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds
as Cofactors. Fukui,T., Kagamiyama, H., Soda, K., Wada, H. (Eds.). Proceedings of the 8thinternational symposium on vitamin B6 and carbonyl catalysis, held in Osaka, Japan, October
15-19. pp. 79-81. International Union of Biochemistry Symposium 1991.
35. Nagatsu, T., Kaneda, N., Kobayashi, K., Ichinose H., Sasaoka, T., Ishii, A., Sumi, C, Kiuchi,
K., Fujita, K., and Kurosawa, Y. (1991).
Genes of human catecholamine-synthesizing enzymes. In: Parkinson's Disease, From ClinicalAspects to Molecular Basis. Nagatsu, T., Narabayashi, H., and Yoshida, M. (Eds.).
Springer-Verlag, Wien, New York, pp. 19-38.
36. Ichinose, H., Katoh, S., Sueoka, T., Titani, K., Fujita, K., and Nagatsu, T. (1992).
Cloning and sequencing of cDNA encoding human sepiapterin reductase. Pteridines, 3(1/2),
41-42.
37. Kobayashi, K., Sasaoka, T., Morita, S., Nagatsu, I., Iguchi, A., Kurosawa, Y., Fujita, K.,
Nomura, T., Kimura, M., Katsuki, M., and Nagatsu, T. (1992).
Genetic alteration of catecholamine specificity in transgenic mice. Proc. Natl. Acad. Sci. USA, 89(5), 1631-1635.
38. Togari, A., Ichinose, H., Matsumoto, S., Fujita, K., and Nagatsu, T. (1992).
Multiple mRNA forms of human GTP cyclohydrolase I. Biochem. Biophys. Res. Commun., 187(1), 359-365.
39. Ogiwara, S., Kiuchi, K., Nagatsu, T., Teradaira, R., Nagatsu, I., Fujita, K., and Sugimoto, T.
(1992 ).
A highly sensitive and specific enzyme liked immunoadsorbent assay of neopterin and biopterin
in biological samples. Clin. Chem., 38(10), 1954-1958.
40. Ichinose, H., Sumi-Ichinose, C., Ohye, T., Hagino, Y., Fujita, K., and Nagatsu, T. (1992).

Tissue-specific alternative splicing of the first exon generates two types of mRNAs in humanaromatic L-amino acid decarboxylase. Biochemistry, 31(46), 11546-11550.
41. Nakano, T., Kobayashi, K., Saito, S., Fujita, K., and Nagatsu, T. (1992).
Mouse dopamine β-hydroxylase-primary structure deduced from the cDNA sequence andexon/intron organization of the gene. Biochem. Biophys. Res. Commun., 189(1), 590-599.
42. Nagatsu, T., Ichinose, H., Katoh, S., Fujita, K., and Titani, K. (1992).
6R-tetrahydrobiopterin biosynthesis: structures of rat and human sepiapterin reductase. J. Nutr.
Sci. Vitaminol. Special Issue, 510-513.
43. Ichinose, H., Sumi-Ichinose, C., Kurosawa, Y., Titani, K., Hagino, Y., Fujita, K., and Nagatsu,
T. (1992).
The gene for human aromatic L-amino acid decarboxylase. In: Advances in Tryptophan Research
1992. Ishiguro, I., Kido, R., Nagatsu, T., Nagamura, Y., Ohta, R. (Eds.). Fuiita Health University
Press, Toyoake, Japan, pp. 37-40.
44. Morita, S., Kobayashi, K., Mizuguchi, T., Yamada, K., Nagatsu, I., Titani, K., Fujita, K.,
Hidaka H., and Nagatsu, T. (1993).
The 5'-flanking region of the human dopamine β-hydroxylase gene promotes neuron
subtype-specific gene expression in the central nervous system of transgenic mice. MolecularBrain Research, 17(3-4), 239-244.
45. Nomura, T., Ichinose, H., Sumi-Ichinose, C., Nomura, H., Hagino, Y., Fujtia, K., and Nagatsu,
T. (1993).
Cloning and sequencing of cDNA encoding mouse GTP cyclohydrolase I. Biochem. Biophys.
Res. Commun., 191(2), 523-527.
46. Nagatsu, I., Yamada, K., Karasawa, N., Kaneda, N., Sasaoka, T., Kobayashi, K., Fujita, K.,
and Nagatsu, T. (1993).
Non-catecholaminergic neuronal expression of human tyrosine hydroxylase in the brain oftransgenic mice with special reference to aromatic L-amino acid decarboxylase. In: Tyrosine
Hydroxylase. From Discovery to Cloning. Naoi, M., Parvez, S.H. (Eds.). VSP, Utrecht, The
Netherlands, pp. 37-57.
47. Nagatsu, T., Kaneda, N., Kobayashi, K., Ichinose, H., Sasaoka, T., Kiuchi, K., Fujita, K., andKurosawa, Y. (1993).
The human tyrosine hydroxylase gene. In. Tyrosine Hydroxylase. From Discovery to Cloning.
Naoi, M., Parvez, S.H. (Eds.). VSP, Utrecht, The Netherlands, pp. 177-191.

48. Ichinose, H., Ohye, T., Takahashi, E., Seki, N., Hori, T., Segawa, M., Nomura, Y., Endo, K.,
Tanaka, H., Tsuji, S., Fujita, K., and Nagatsu, T. (1994).
Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations of the GTP
cyclohydrolase I gene. Nature Genetics, 8(3), 236-242.
49. Kobayashi, K., Morita, S., Mizuguchi, T., Sawada, H., Yamada, K., Nagatsu, I., Fujita, K.,
and Nagatsu, T. (1994).
Functional and high-level expression of human dopamine β-hydroxylase in transgenic mice. J.
Biol. Chem., 269(7), 29725-29731.

－新規臨床検査法の開発ならびにその適用－
1. Keisuke Fujita, Masamitsu Oguri, Tetsuhiko Mizuno, Ikuko Sakaki. (1957).
On the changes of the ninhydrin-Schiff reaction of protein solutions by treatment with urea
solution. Nagoya Journal of Medical Science 19: 155-159.
2. 藤田啓介 (1958).
電気泳動技術の新しい試み. 現代医学, 5, 217-228.
3. 小原喜重郎, 及川正信, 藤田啓介, 葛谷博磁 (1962).
黒血症赤血球の濾紙電気泳動図. 日本血液学雑誌, 25, 739-742.
4. 藤田啓介 (1975).
若い臨床検査技師に望むことなど. 検査と技術, 3(4), 5-8, 64.
5. Fujita, K., Yamada, K., Sato, T., Takagi, I., and Sakashita, T. (1977).
A rapid method for embedding biological tissues in a low viscosity epoxy resin "Quetol 651" forelectron microscopy. J. Electron Microsc., 26, 165-166.
6. Fujita, K., Hirano, M., Ochiai, J., Funabashi, M., Nagatsu, I., Nagatsu, T., and Sakakibara, S.
(1978).
Serum glycylproline p-nitroanilidase activity in rheumatoid arthritis and systemic lupus
erythematosus. Clin. Chim. Acta, 88, 15-20.
7. Fujita, K., Hirano, M., Tokunaga, K., Nagatsu, I., Nagatsu, T., and Sakakibara, S. (1977).
Serum glycylproline p-nitroanilidase activity in blood cancers. Clin. Chim. Acta, 81, 215-217.
8. Kato, T., Iwase, K., Nagatsu, T., Sakakibara, S., and Fujita, K. (1979).
Comparison of X-prolyl dipeptidyl-aminopeptidase activity in human cerebrospinal fluid with thatin serum. Experientia, 35, 20-21.
9. Kato, T., Nakano, T., Nagatsu, T., Fuyamada, H., Hino, M., Takahashi, H., and Fujita, K.
(1979).
X-Prodipeptidyl-aminopeptidase activity in serum and tissues of SHR and SHRSP. Jpn. Heart J.
(Suppl. 1), 20, 331-333.
10. Ito, S., and Fujita, K. (1980).
Detection of thiols on thin-layer chromatograms with 3,5-di-tert.-butyl-l,2-benzoquinone-iron(Ⅲ)
chloride. J. Chromatogr., 187, 418-420.
11. Ito, S., Maruta, K., Imai, Y., Kato, T., Ito, M., Nakajima, S., Fujita, K., and Kurahashi, T.
(1982).
Urinary p-aminobenzoic acid determined in the pancreatic function test by liquid chromatography,
with electrochemical detection. Clin. Chem., 28, 323-326.
12. 藤田啓介, 山田保雄 (1982).
Meldola Blue 法による Lactobacillus の Lactic Dehydrogenase 電気泳動分析. 医学と生物学,
105, 191-194.
13. Fujita, K., Maruta, K., Ito, S., and Nagatsu, T. (1983).
Urinary 4-hydroxy-3-methoxymandelic (vanillylmandelic) acid,
4-hydroxy-3-methoxyphenylacetic (homovanillic) acid, and 5-hydroxy-3-indoleacetic aciddetermined by liquid chromatography with electrochemical detection. Clin. Chem., 29, 876-877.
14. Maruta, K., Fujita, K., Ito, S., and Nagatsu, T. (1984).
Liquid chromatography of plasma catecholamines, with electrochemical detection, after treatment
with boric acid gel. Clin. Chem., 30,
1271-1273.
15. 加藤寿章, 伊藤祥輔, 藤田啓介, 神保孝一 (1984).
尿中カテコールアミン"全''酸化代謝物の定量－年齢別正常値と神経芽細胞腫および悪性黒色腫の検討－. 藤田学園医学会誌, 8, 345-348.
16. 伊藤圓, 大谷元彦, 落合潤一, 厚味高弘, 勅使河原深雪, 山内 実, 藤田啓介 (1984).

藤田学園保健衛生大学病院と第二病院との臨床検査情報交換システム. 臨床検査とコンピ
ュータ, '84 ～'85, 69-74.
17. Iwase-Okada, K., Nagatsu, T., Fujita, K., Torikai, K., Hamamoto, T., Shibata, T., Maeno, Y.,
and Sakakibara, S. (1985).

Serum collagenase-like peptidase activity in rheumatoid arthritis and systemic lupus
erythematosus. Clin. Chim. Acta, 146, 75-79.
18. Ito, S., Kato, T., Maruta, K., Jimbow, K., and Fujita, K. (1985).
"Total"acidic metabolites of catecholamine in urine as determined by hydrolysis with hydriodic
acid and liquid chromatography: application to patients with neuroblastoma and melanoma. Clin.
Chem., 31, 1185-1188.
19. 堀場重幸, 岡村和彦, 山本恵申, 井上茂樹, 伊藤 圓, 藤田啓介 (1985).
ラテックス近赤外比濁分析方法(LPIA 法)を応用した高感度免疫血清検査法の検討. 衛生検査, 34(10), 1453-1460.
20. Ito, S., Fujita, K., Yoshioka, M., Sienko, D., and Nagatsu T. (1986).
Identification of 5-S and 2-S-cysteinyldopamine and 5-S-glutathionyldopamine formed fromdopamine by high-performance liquid chromatography with electrochemical detection. J.
Chromatogr., 375, 134-140.
21. Ito, S., Kato, T., and Fujita, K. (1986).
Determination of urinary 5-S-cysteinyldopamine by high-performance liquid chromatography withelectrochemical detection. Chromatographia, 21, 645-647.
22. Kojima, K., Mihara, R., Sakai, T., Togari, A., Matsui, T., Shinpo, K., Fujita, K., Fukasawa,
K., Harada, M., and Nagatsu, T. (1987).
Serum activities of dipeptidyl-aminopeptidase II and dipeptidyl-aminopeptidase IV intumor-bearing animals and in cancer patients. Biochem. Med. Metab. Biol., 37, 35-41.
23. Imai,Y., Ito, S., and Fujita, K. (1987).
Determination of natural thiols by liquid chromatography after derivatization with
3,5-di-tert.-butyl-1,2-benzoquinone. J. Chromatogr., 420, 404-410.
24. Imai, Y., Ito, S., Maruta, K., and Fujita, K. (1988).
Simultaneous determination of catecholamines and serotonin by liquid chromatography, after
treatment with boric acid gel. Clin. Chem., 34, 528-530.

－その他－
1. 工藤祐三, 藤田啓介他 (1962).
岩手医科大学 C.P.C.記録－咳嗽と貧血を主症状とし,された 1 例. 岩手医学雑誌, 14, 23-31.

肺粟粒結核症か肺癌かの診断に迷わ2. 鶴田光敏, 小沢 徹, 児玉 央, 金森俊輔, 宮田隆夫, 矢崎雄彦, 篠原靖忠, 川井 薫, 丸田
一裕, 伊藤祥輔, 藤田啓介 (1985).
喘息児の交感神経機能－カテコールアミンの日内変動について－. 藤田学園医学会誌, 9,451-456.
3. 丸田一皓, 高橋久英, 藤田啓介 (1989).
Non-Obese-Diabetic (NOD) ハツカネズミ脾細胞における幼若化反応の異常. 医学と生物学,
118(5), 327-330.
4. 藤田啓介 (1989).
病院医療運営管理の合理化を目的とした診療情報トランザクション･システムの構築. 医療
情報学, 9, 349-358.
5. Mogi, M., Harada, M., Kojima, K., Adachi, T., Narabayashi, H., Fujita, K., Naoi, M., andNagatsu, T. (1989).
β 2-Microglobulin decrease in cerebrospinal fluid form parkinsonian patients. Neurosci. Lett.,
104, 241-246.
6. Tsuruta, M., Kozawa, T., Miyata, T., Yazaki, T., Ito, S., Nagatsu, T., and Fujita, K. (1989).
Differences in the response if circulating noradrenaline and adrenaline in exerciseinduced asthma.
Biogenic Amines, 6, 75-80.
7. Kozawa, T., Urisu, A., Yazaki, T., Tsuruta, M., Ito, S., Nagatsu, T., and Fujita, K. (1989).
Relationship between severity of asthma and response of noradrenaline and adrenaline to exercise.
Biogenic Amines, 6, 301-308.
8. Sugimoto, T., Ogiwara, S., Kiuchi, K., Nagatsu, T., Masao, S., and Nagatsu, I., Fujita, K.
(1990).
An enzyme immunoassay for neopyerin and biopterin using a microtitre plate linked with N2-(3aminopropyl) derivatives of pteridines. Pteridines, 2, 141-146.
9. Nakajima, T., Ando, Y., and Fujita, K. (1992).
Lateral low-frequency components of reflected sound from a canopy complex comprising
triangular plates in concert halls. J. Acoust. Soc. Am., 92(3), 1443-1451.
10. 小畑雅史, 新保 寛, 舟橋正範, 藤田啓介, Luchetta, R., Winter, W.E. (1992).
[(NOD/Uf × NZW)F1 × NOD/Uf] 第 1 代戻し交配マウスにおける膵島炎の発症とα, β,γ T 細胞レセプター遺伝子の相関性. 医学と生物学, 125(6), 245-249.

11. 小畑雅史, 新保 寛, 舟橋正範, 藤田啓介, Cheng, I., Luchetta, R., Winter, W.E. (1992).
[(NOD/Uf × NZW)F1 × NOD/Uf] 第 1 代戻し交配マウスにおける膵島炎の発症と第 9 染色体遺伝子マーカー（Thy-1 および P3-450）の相関性. 医学と生物学, 125(6), 251-254.
12. Mogi, M., Harada, M., Riederer, P., Narabayashi, H., Fujita, K., and Nagatsu, T. (1994).
Tumor necrosis factor-α (TNF-α) increases both in the brain and in the cerebrospinal fluid
from parkinsonian patients. Neurosci. Lett., 165(1, 2), 208-210.

【国際学会､国際会議､シンポジウム】
1. Fujita, K., Ito, T., Maruta, K., Teradaira, R., Beppu, H., Nakagami, Y., Kato, Y., Nagatsu, T.,
and Kato,T. (1978).
Serum dopamine β-hydroxylase in schizophrenic patients. Fourth International Catecholamine
Symposium, September 17-22.
2. Teradaira, R., Fujita, K., Inoue, T., Takahashi, H., Yagyu, S., and Nagatsu, T. (1981).
In vivo dopamine β-hydroxylase activity in spontaneously hypertensive rats: Changes by stress.
The Fourth International Symposium on Rats with Spontaneous Hypertension and Related Studies,
Heiderberg, September 2-4.
3. Nagatsu, T., Oka, K., Ashiba, G., Kiss, B., Fujita, K., Teradaira, R., and Takahashi, H.
(1983).
Stress-induced changes in In vivo and in vitro activity of catecholamine-synthesizing enzymes.
Third Symposium on Catecholamines and Other Neurotransmitters in Stress. Czechoslovakia,
June 7-12.
4. Nagatsu, I., Ito, M., Kawakami, Y., Karasawa, N., Takahashi, H., Fujita, K., and Nagatsu, T.
(1984).
The quantitative immunoenzyme-histocytochemistry of tyrosine hydroxylase in the brain of
spontaneously hypertensive rats. Abstracts of The Seventh Annual Meeting of The Japan
Neuroscience Society, Neuroscience Letters Supplement 17, S121.
5. Nagatsu, T., Sinpo, K., Kawai, K., Shinzato, M., Ito, S., Matsui, T., Nakamura, K., Kitagawa,Y., Hirano, M., Ito, M., and Fujita, K. (1984).
Acetylpolyamines in urine and polyamines in erythrocytes as biochemical markers of cancer.
Polyamines: Basic and Clinical Aspects-A Satellite Symposium of The 3rd International Congress
on Cell Biology (Abstracts), 29.
6. Ito, S., and Fujita, K. (1980).
Phaeomelanogenesis in the absence of tyrosinase. The XIth International Pigment Cell

Conference, 28.
7. Fujita, K., Izawa, Y., Beppu, H., Ito, S., Shinzato, M., Ueda, H., and Inasaka, H. (1980).
Effects of high molecular aloe components on thermal burns. Regional Meeting for Burn Injuries
in Japan. Program and Abstracts, 55.
8. Teradaka, R., Fujita, K., Nagatsu, T., Shinpo, K., Maruta, K., and Nakamura, M. (1980).
Analysis for urinary polyamines in cancer patients by a simple and rapid high-voltage paper
electrophoretic method. Joint Congress of the Scandinavian and German Societies of Clinical
Chemistry, Hamburg, October 8-11, 1980, Journal of Clinical Chemistry and Clinical
Biochemistry, 18, 698.
9. Ito, S., Fujita, K., Takahashi, H., Maeda, K., and Jimbow, K. (1983).
Characterization of melanogenesis in mouse hair by chemical analysis of melanins and of freeand bound dopa and 5-S-cysteinyldopa. The XIIth International Pigment Cell Conference, 94.
10. Ito, S., Jimbow, K., Kato, T., Kiyota, M., and Fujita, K. (1983).
Protein-Bound dopa and 5-S-cysteinyldopa in melanogenic and non-melenogenic tissues. The
XIIth International Pigment Cell Conference, 95.
11. Ito, S., Kato, T., Maruta, K., Kurahashi, T., and Fujita, K. (1984).
Determination of dopa, dopamine, 5-S-cysteinyldopa in plasma, urine, and tissue samples byhigh-performance liquid chromatography with electrochemical detection. Japanese Society for
Investigative Dermatology, IXth Annual Meeting, 72.
12. Ito, S., and Fujita, K. (1984).
Microanalysis of eumelanin and pheomelanin in hair and melanomas by chemical degradations.
Vth European Workshop on Melanin Pigmentation, 21.
13. Kato, T., Ito, S., and Fujita, K. (1986)
Tyrosinase-catalyzed binding of catechols with proteins through the sulfhydryl group. Proceedingsof the XIIIth International Pigment Cell Conference, Tusson, Arizona, October 5-9, 1986.
Abstract: J. Invest. Dermatol., 87.
14. Inoue, S., Hasegawa, K., Ito, S., Wakamatsu, K., and Fujita, K. (1990).
Binding to melanin enhances the cytotoxicity of 4-S-cysteaminylphenol. Proceedings of XIV
International Pigment Cell Conference, Kobe, Japan, October 31-November 4.
15. Shimpo, K., Nagatsu, T., Yamada, K., Sato, T., Niimi, H., Shamoto, M., Takeuchi, T.,
Umezawa, H., and Fujita, K. (1990).

Ascorbic acid and adriamycin toxicity. Ascorbic Acid:Biological Functions and Relation to
Cancer, Program and Abstracts, p.77 National Institutes of Health, Bethesda, Maryland,
September 10-12.
16. Obata, M., Ito, S., Beppu, H., Nagatsu, T., and Fujita, K. (1991).
Mechanism of anti-inflammatory and anti-thermal burn action of Aloe arborescens Mill. var.
natalensis Berger. International Congress of Phytotherapy, Seoul Korea, October 16-17.
17. Beppu, H., and Fujita, K. (1991).
Isolation and the pharmacological activities of the effective compounds from Aloe arborescens
Mill. var. natalensis Berger. International Congress of Phytotherapy, Seoul Korea, October 16-17.
18. Ito, S., Teradaira, R., Beppu, H., Obata, M., Nagatsu, T., and Fujita, K. (1991)
Properties and pharmacological activity of carboxypeptidase in Aloe arborescens Mill. var.
natalensis Berger. International Congress of Phytotherapy, Seoul Korea, October 16-17.
19. Beppu, H., Nagamura, Y., and Fujita, K. (1991).
Hypoglycemic and anti-diabetic effects of Aloe arborescens Mill. var. natalensis Berger.
International Congress of Phytotherapy, Seoul Korea, October 16-17.
20. Kawai, K., Beppu, H., Marunouchi, T., Koike, T., and Fujita, K. (1991).
Tissue culture of Aloe arborescens Mill. var. natalensis Berger. International Congress of
Phytotherapy, Seoul Korea, October 16-17.
21. Tsuda, H., Ito, M., Hirono, I., Kawai, K., Beppu, H., Fujita, K., and Nagao, M. (1991).
Inhibitory effect of Aloe arborescens Mill. var. natalensis Berger (ALOE) on induction ofpreneoplastic focal lesions in the rat liver. International Congress of Phytotherapy, Seoul Korea,
October 16-17.
22. Teradaira, R., Shinzato, M., Beppu, H., and Fujita, K. (1991).
Anti-gastoric ulcer effects of Aloe arborescens Mill. var. natalensis Berger. International
Congress of Phytotherapy, Seoul Korea, October 16-17.
23. Hasegawa, K., Inoue, S., Wakamatsu, K., Ito, S., Fujita, K., and Ishihara, K. (1993).
Changes in plasma 5-S-cysteinyldopa in melanoma-bearing mice treated with interferon-β or
DTIC. Proceedings of XVth International Pigment Cell Conference, London, U.K., September
26-30. Abstract: Pigment Cell Research, 6, 291.
24. Shimpo, K., Takahashi, H., Tsuda, H., Hibino, S., Kawai, K., Kimura, C., Nagatsu, T., andFujita, K. (1993).

Inhibition of hepatocarcinogenesis in ODS rats fed on 3'-methyl-4-dimethylaminoazobenzene by
2-O-octadecylascorbic acid, ascorbyl palminate and ascorbic acid. The 8th International
Symposium on Prevention and Detection of Cancer, Nice, France, March 14-16. Abstract: Cancer
Detection and Prevention, 17/1, CRC Press, Pearl River, NY, 128.

【国内学会】
1. 藤田啓介 (1952).
家鶏肉腫の増殖に関する生化学的研究(第 1 報). 名古屋医学, 66, 243.
2. 藤田啓介, 松原敏夫 (1952).
家鶏肉腫の増殖に関する生化学的研究(第 2 報). 名古屋医学, 66, 432-433, 1952.
3. 藤田啓介, 石黒伊三雄, 松原敏夫, 松井博, 岩瀬正次 (1953).

トリパン青による制癌の生化学的機構. 生化学, 26, 415-416.
4. 藤田啓介, 岩瀬正次 (1953).
家鶏肉腫の増殖に関する生化学的研究(第 3 報). 名古屋医学, 67, 311.
5. 藤田啓介, 石黒伊三雄 (1953) .
発癌過程における代謝像のありさま. 名古屋医学, 68, 707-708.
6. 堀田一雄, 藤田啓介, 石黒伊三雄 (1954) .
トリパン青による制癌の際のビタミン B2 の態度. ビタミン, 7, 803-804.
7. 堀田一雄, 藤田啓介, 石黒伊三雄 (1954) .
肝癌組織における FAD-ase について（予報). ビタミン, 7, 804.
8. 藤田啓介, 石黒伊三雄 (1954) .
肝癌組織の FAD-ase について（予報). ビタミン, 7, 897.
9. 藤田啓介, 石黒伊三雄 (1954) .
トリパン青による制癌の際のビタミン B2 の態度. ビタミン, 7, 897.
10. 藤田啓介, 岩瀬正次 (1954) .
家鶏肉腫粘液多糖類の生物学的意義. 癌, 45, 116-117.
11. 岩瀬正次, 藤田啓介 (1954) .
ラッテの DAB 発癌過程に及ぼすトリパン青の影響. 癌, 45, 383-386.

12. 岩瀬正次, 藤田啓介 (1955) .
ラッテの DAB 発癌過程に及ぼすトリパン青及びトリパン赤の影響. 癌, 46, 352-354.
13. 小栗正光, 藤田啓介, 水野哲彦, 高柳哲也 (1956) .
腎疾患の血清蛋白及び尿蛋白のアミノ酸並びにカルボキシル基について. 名古屋医学, 71,
286-287.
14. 高柳哲也, 内田利江, 藤田啓介 (1956) .
魚類血合筋, 並びに普通筋の組織蛋白について（予報）. 名古屋医学, 71, 287.
15. 堀田一雄, 藤田啓介, 新井豊久 (1956) .
濾紙上の螢光物質に対する写真撮影の試み. ビタミン, 10, 527.
16. 塚本英世, 藤田啓介, 小栗正光, 水野哲彦, 高柳哲也, 杉山泰世 (1956) .
白血病白血球の蛋白の性状について. 名古屋医学, 72, 92.
17. 石黒伊三雄, 藤田啓介, 塚本英世, 新井豊久 (1956) .
白血病の尿中盲螢光物質について. 名古屋医学, 72, 92.
18. 清水浩光, 藤田啓介 (1957) .
実験的腫瘍および人白血病細胞の Glucose-6-phosphatase Activity にいて. 癌, 48, 594-596.
19. 藤田啓介, 小栗正光 (1958) .
蛋白変性とニンヒドリン－シッフ反応, 特に癌動物血清についての試み. 名古屋医学, 76,436.
20. 藤田啓介, 石田 徹, 谷口清昭, 所美枝子, 駒野博子, 橋川豊子, 小水寿美子 (1969).
ラットの膵及び尿糖に及ばすニンヒドリンの影響. 第 1 回名古屋保健衛生学会講演抄録集,
8.

【特

許】

1. 藤田啓介 (1996).
ユリ科アロエ属に属する植物の真空凍結乾燥体を利用した錠剤製品及びその製造方法. 日
本国, 特許公報（B2）, 特許番号 第 2514102 号, 登録日 1996/04/30
2. Fujita, K. (2002).
Tableted product prepared by vacuum freeze-drying of a plant belonging to genus Aloe of family
liliaceae and the method for producing same. United States Patent, Patent No.:US6,368,624 B1
Date of Patent: Apr. 9, 2002

3. Fujita, K. (2002).
Tableted product prepared by vacuum freeze-drying of a plant belonging to genus Aloe of family
liliaceae and the method for producing same. United States Patent, Patent No.:US6,399,095 B1
Date of Patent: Jun. 4, 2002

【映画】

1) 「Hemispherectomy」（全 20 分）昭和 37 年製作.
2) 「明日を開く医療」（全 35 分）昭和 55 年 12 月 20 日製作.
3) 「先進の医療情報システム」（同上）昭和 60 年 7 月 31 日製作.