bluuebunny/crossref_metadata_2025_split huggingface dataset:
Measurement of serum myoglobin by a turbidimetric latex agglutination method
Authors: Uji Yoshinori , Okabe Hiroaki , Sugiuchi Hiroyuki , Sekine Sakari 
Published: March 2007

AbstractWe evaluated an immunoturbidimetric quantitation for serum myoglobin by the latex agglutination method using an automated biochemical analyzer. This method is rapid, specific, accurate, precise, and has wide dynamic range. The total assay time is 10 min and is performed at 37°C with continuous monitoring at 570 nm.The assay results were compared with radioisotopic immunoassay results and showed a good correlation coefficient, r= 0.99; Y = 0.98× + 9.3; N = 79. Sera from healthy adults has a myoglobin concentration in the range of 15‐80 ng/ml(N=362). Sex‐and age‐related differences were observed. The serum myoglobin levels in males and elderly people showed higher concentration than in females and younger people. The peak elevation of serum myoglobin compared with other cardiac markers was observed within 6 hours after onset of chest pain as well as the CK‐isoform ratio (MM3/MM1). All of the serum from 21 patients with definite acute myocardial infarction showed increased serum myoglobin levels (100‐1200 ng/ml) upon admission and within 6 hours.The results suggest that assays for serum myoglobin levels are helpful in the early diagnosis of acute myocardial necrosis.
Determination of aluminum in biological fluids by furnace atomic absorption spectrophotometry
Authors: Johnson Keith E. , Treble Ronald G. 
Published: March 2007

AbstractDetailed procedures were developed forth furnace atomic absorption spectrophotometry (FAAS) determination of aluminum (Al) in serum, urine, cerebrospinal fluid (CSF), and proportionated dialysate. Of particular note were the use of Mg (NO3)2.6H2O as a matrix modifier and the employment of the standard additions routine in analysis. The accuracy of the method(s) used is supported by work with assayed controls and by recovery studies. The use of a “clean room” was shown to be unnecessary. Normal serum, urine, and CSF Al ranges observed were 4.8–8.9, 5.1–9.1 adn 1.0–5.8μgL −1 respectively. © 1992 Wiley‐Liss, Inc.
G test, a new direct method for diagnosis of Candida infection: Comparison with assays for beta‐glucan and mannan antigen in a rabbit model of systemic candidiasis
Authors: Miyazaki Takashige , Kohno Shigeru , Koga Hironobu , Kaku Mitsuo , Mitsutake Kotaro , Maesaki Shigefumi , Yasuoka Akira , Hara Kohei , Tanaka Shigenori , Tamura Hiroshi 
Published: March 2007

AbstractAn indirect method to measure betaglucan, a major structural component of yeast cell walls, is available, but has the disadvantage of requiring the combined use of two assays. Recent reports describe the fungal index, which measures the difference between the conventional limulus test, in which factors C and G react with endotoxin and beta‐glucan, and a new endotoxin‐specific test, in which only factor C reacts with endotoxin. The G test was developed as a direct method to measure beta‐glucan alone. In this study, the G test was examined in sera of rabbits with experimental systemic candidiasis, and compared with the fungal index and mannan assay.The G test showed positive in all rabbits with systemic candidiasis faster and with higher titers than with the fungal index. Three rabbits with fulminant systemic candidiasis showed higher levels of reactivity with the G test and the fungal index than two rabbits with mild reactions. Mannan was positive by at least one serum in four of five rabbits by the latex agglutination test, and there was a good correlation between these assays. The G test is a good serodiagnositc method for the detection of candidiasis. © 1992 Wiley‐Liss, Inc.
Stability of respiratory syncytial virus antigen due to buffer treatment for direct detection in nasopharyngeal specimens with enzyme immunoassay
Authors: Döller G. , Schuy W. 
Published: March 2007

AbstractWe developed an enzyme immunoassay (direct EIA; Enzygnost®RSV[Ag]) for the direct detection of respiratory syncytial virus (RSV) antigen in nasopharyngeal specimens (NPS). The test procedure is the same as our recently described direct EIA for detection of influenza A and B virus antigens in NPS. For practical purposes it is of advantage to differentiate respiratory viruses on the same microtitration plate in the same run. The test shows no limitations by sample consistency, and results are obtained within 4 hr. In contrast to other test systems, sonification is not necessary. This is due to the sample buffer STD. We studied the influence of sample buffer STD on the stability of RSV (strain Long) antigen at different temperatures over a period of 7 days. PBS‐BSA‐buffer served as control. The treatment and storage of RSV (strain Long) with sample buffer STD at room temperature or at 4ˆC showed no decrease of antigen detectability. The antigen is very stable in contrast to the storage of RSV (strain Long) in PBS‐BSA buffer during the observation period of 7 days. Consequently, when NPS are stored in sample buffer STD, results of direct EIA are independent from the time of transport and temperature within 7 days.Thirty‐eight NPS from infants with confirmed RSV infection were investigated. Confirmation was performed by virus isolation (n = 29) or with commercially available enzyme immunoassays or immunofluorescence test (n = 9). The direct EIA showed a specificity of 99.3% (n= 140) and a sensitivity of 95% (n = 38). © 1993 Wiley‐Liss, Inc.
Detection of the extracellular domain of c‐erbB‐2 oncoprotein in sera from patients with various carcinomas: Correlation with tumor markers
Authors: Wu James T. , Astill Mark E. , Zhang Ping 
Published: March 2007

AbstractUsing a serum enzyme immunoassay (EIA) kit from Triton diagnostics we detected c‐erbB‐2 oncoprotein activity in random sera containing highly elevated tumor markers and also in serial specimens from cancer patients expressing elevated oncoprotein activities. Elevated oncoprotein activity was found not only in sera of breast and ovarian carcinomas but also in sera from colorectal, pancreatic, and prostate carcinomas and even from primary hepatoma. Whenever oncoprotein was overexpressed in an individual patient, there was usually an excellent correlation between the oncoprotein activity and the level of dominant tumor marker in serial serum specimens. Based on the size exclusion S‐200 column chromatography, we found only a single molecule containing c‐erbB‐2 oncoprotein activity in pooled sera from cancer patients whereas two oncoproteins slightly different in size were detected in breast tumor tissue cytosol. Using HPLC on a Superose 12 HR column, the serum portion of the oncoprotein was eluted at a position near IgG, suggesting that the extracellular domain of the oncoprotein exists as a dimer in the serum. © 1993 Wiley‐Liss, Inc.
Analysis of human sera for filarial IgM antibody using antigen fractions isolated from immune complexes
Authors: Prasad G. B. K. S. , Harinath B. C. 
Published: March 2007

AbstractFilarial IgM antibody response to various antigenic fractions isolated from immune complexes by SDS‐PAGE viz., IC‐2, IC‐4, IC‐7, and IC‐9, was studied by ELISA. The IgM antibody response to almost all antigenic fractions was seen more in microfilaraemic group compared to the clinical filariasis group. The antibody response to IC‐9 antigen fraction as compared to other fractions was found significantly higher in microfilaraemic patients than in patients with clinical manifestations. Ninety percent of microfilariae carriers and 75% of clinical filarial patients have shown IgM isotype to IC‐9 antigen. Studies with various lectins have revealed the Con A binding nature of IC‐9 antigen. This study suggests that IC‐9 antigen could be another candidate antigen in the immunodiagnosis of lymphatic filariasis. © 1993 Wiley‐Liss, Inc.
Marking characteristics of anti‐nuclear matrix protein NM200.4 in human breast carcinomas and normal human tissues
Authors: Wisecarver James L. , Synovec Mark S. , Pirrucello Sam , Linder James 
Published: March 2007

AbstractNuclear matrix proteins are a group of recently described proteins that are thought to be cell‐type specific. Using a monoclonal antibody (NM 200.4; Matritech, Cambridge, MA) generated against nuclear matrix proteins isolated from a human breast carcinoma cell line, we examined frozen tissue sections from 30 breast carcinomas, and a variety of normal tissues to determine the antibody specificity, and to assess the relationship with the staining pattern and tumor type and hormone receptor status. Most breast carcinomas marked with the antibody, but stromal and vascular endothelial cells in the tissues surrounding these lesions also marked focally. Marking of vascular endothelium in a variety of benign tissues, renal tubular epithelium, and occasionally uterine smooth muscle cells was also observed. Normal breast tissue from 4 patients without breast cancer did not react. Studies on breast tumors revealed that 15/20 invasive ductal, 3/4 in situ ductal, 3/3 medullary, 2/2 invasive lobular, and 1/1 colloid carcinomas marked with this antibody. Image analysis revealed that the staining intensity of medullary carcinoma was twice that found in invasive ductal carcinoma (avg pixel density 76.6 vs. 30.1; P <0.05). Invasive lobular and in situ ductal carcinoma also expressed higher staining intensities than invasive ductal carcinoma, but these differences were not significant. Invasive ductal carcinomas had heterogeneity in staining intensity (avg. pixel intensity range: 0‐94 units). Tumors with multiple aneuploid populations had significantly higher stain intensity values than either diploid lesions or lesions containing a single aneuploid population (P <0.05). Nuclear grade did not correlate with staining intensity. No significant correlation was found between the image analysis values and either the estrogen or progesterone receptor content of the lesions as determined by charcoal‐ligand binding bioassay. Our studies indicate that a monoclonal antibody to such a protein may be useful in defining a subset of breast carcinomas. © 1993 Wiley‐Liss, Inc.
In situ hybridization for epidermal growth factor receptor (EGFR) external domain transcripts in prostatic adenocarcinoma
Authors: Montone Kathleen T. , Tomaszewski John E. 
Published: March 2007

AbstractWe examined prostatic adenocarcinomas from 19 formalin fixed radical prostatectomy specimens for EGFR by in situ hybridization employing a 24 base synthetic biotin‐labeled oligonucleotide probe complementary to the 5' end of EGFR mRNA. All slides were examined by light microscopy using a 25 × objective. Each field was given three values: 1) Gleason grade (1‐5), 2) Nuclear grade [small (<5.0 μ), intermediate (5‐10 μ), large (>10 μ)], and 3) EGFR staining intensity score (0, absent; 1, weak; 2 +, moderate to strong). A total 851 25 × fields of prostatic adenocarcinoma were studied. All cancers demonstrated at least some degree of cytoplasmic EGFR message. The EGFR intensity score correlated best with tumor nuclear size. No correlation with Gleason grade was observed. Cytoplasmic staining was also identified in the basal cell layer of benign glands, high grade prostatic intraepithelial neoplasia, stromal nodules, transitional epithelium, periurethral glands, and ganglion cells. Competitive hybridization experiments using an unlabeled EGFR probe showed markedly diminished hybridization signal, while in situ hybridization with a biotin‐labeled EGFR sense probe was negative. Immunohistochemistry on 13 of the tumors with 2 monoclonal antibodies against EGFR showed staining in only 1/13 and 10/13 tumors. EGFR expression appears to be most prominent in tumors of high nuclear grade. Further studies will be necessary to explore this growth factor as a prognostic variable in this tumor. © 1993 Wiley‐Liss, Inc.
Prostate‐specific antigen and prostate volume: A meta‐analysis of prostate cancer screening criteria
Authors: Aziz Douglas C. , Barathur Raj B. 
Published: March 2007

AbstractObjective: To establish the value of serum prostate‐specific antigen (PSA) and prostatespecific antigen per unit volume of prostate gland (PSAD) in detecting prostate carcinoma (CaP) in a hypothetical screening algorithm, a meta‐analysis of the sensitivities, specificities, predictive values and likelihood ratios were combined from the published data.Data Sources: Journal articles identified by a MEDLINE database search from 1988 to October 1992, using prostate‐specific antigen as a key word were used to calculate the distribution of PSA in healthy men, men with benign prostatic hyperplasia (BPH) and men with prostate carcinoma (CaP)Study Selection: Only studies that contained the specified serum PSA values and patient outcomes were included.Data Extraction: The distributions of the serum PSA were plotted versus serum PSA for healthy men (2567), men with BPH (798) and men with CaP (835) from the abstracted data. Prostate volume distributions were estimated from the published transrectal ultrasound (TRUS) calculations.Data Synthesis: Hypothetical cohorts of 1,000 men between the ages of 60 and 70 years were screened using three different screening decision algorithms. Using a serum PSA cutoff of 3.0 ng/ml for referral for transrectal biopsy, 59 of 80 (74%) CaP would be detected and 21 (26%) would be missed. 209 transrectal biopsies would be performed, and 150 (72%) of them would be negative for CaP. Using a serum PSA cutoff of 4.0 ng/ml, 52 of 80 (65%) CaP would be detected and 28 (35%) would be missed. 146 transrectal biopsies would be performed, and 94 (64%) of them would be unnecessary. Using a cutoff of 2.0 ng/ml for serum PSA and 0.1 ng/ml/cc for PSAD, 55 of 80 (69%) of the cancers would be detected and 25 (31%) would be missed. Only 84 transrectal biopsies would be performed, and 29 (35%) of them would be negative for cancer.Conclusion: This algorithm maximizes the number of cancers detected (true‐positive cases) and at the same time reduces the number of false‐positive cases, minimizing the number of patients who would have to receive an unnecessary transrectal biopsy, compared to using a serum PSA cutoff of 3.0 or 4.0 ng/ml. © 1993 Wiley‐Liss, Inc.
Rapid measurement of serum pancreatic amylase
Authors: Landt Michael , Hortin Glen L. , Smith Carl H. , Pashos Gail , Vaidya Hemant C. , Rosenblum Jerry L. 
Published: March 2007

AbstractA simple, rapid assay for the pancreatic isoenzyme of human serum amylase was developed. The assay utilized an immunoabsorbent prepared by coating latex beads with a monoclonal antibody specific for pancreatic amylase. Treatment of patient serum with immunoabsorbent removed pancreatic amylase, and measurement of residual amylase activity with standard total amylase methodology allowed estimation of the pancreatic amylase content. Extraction efficiency of pancreaticamylase was consistent at amylase concentrations up to 1,000 U/L (y = 0.97 × + 16.7 U/L; r = 0.9995). The assay was standardized with purified pancreatic amylase added to neonatal serum (low endogenous activity). A comparison of patient specimen results with the results of a standard technique (cellulose acetate electrophoresis) yielded an excellent correlation (immunoabsorption result = 0.96 electrophoresis result + 1.2 U/L; r = 0.987). Salivary amylase did not interfere with the assay until levels exceeded 1,000 U/L. Daily analysis of a frozen serum pool yielded a coefficient of variation of 9.2% at mean pancreatic amylase value of 54 U/L (±5 U/L). A normal range study found a strong influence of age, with pancreatic amylase levels increasing dramatically in the first 3 years of life, to stabilize at a range of 0–66 U/L thereafter. © 1994 Wiley‐Liss, Inc.
A new immunoassay for the measurement of myoglobin in serum
Authors: Carraro P. , Plebani M. , Varagnolo M. C. , Zaninotto M. , Rossetti M. , Burlina A. 
Published: March 2007

AbstractBecause the concentration of serum myoglobin (Mb) increases within 2 to 4 hours after the first sign of acute myocardial infarction, it has been proposed as an early marker of the condition. Our aim was to evaluate a new assay that provides a rapid, quantitative determination of Mb (Baxter Stratus Myoglobin) based on the radial partition technique. We compared the results obtained by this technique with those from nephelometric and radioimmunoassay methods. A significant agreement was observed, the correlation coefficients (r) being 0.999 and 0.996, respectively. The method evaluated provided good reproducibility with CVs between 3.14% and 4.87%, and its linearity and analytical sensitivity were satisfactory. The clinical evaluation of this assay demonstrates that Mb increases in serum of patients with acute myocardial infarction before total creatine kinase and creatine kinase MB isoenzyme. Mb concentration shows an early peak and earlier return to normal values after the necrosis compared to enzymatic activities. Moreover the assay is rapid and fully automated. The method is therefore considered appropriate for contributing to the early diagnosis of AMI in clinical laboratories. © 1994 Wiley‐Liss, Inc.
Alteration of aldolase isozymes in serum and tissues of patients with cancer and other diseases
Authors: Asaka Masahiro , Kimura Toshio , Meguro Takashi , Kato Mototsugu , Kudo Mineo , Miyazaki Tamotsu , Alpert Elliot 
Published: March 2007

AbstractWe studied the alteration of aldolase isozymes in the serum and tissues of patients with cancer and other diseases using radioimmunoassays specific for aldolaseA, B, and C subunits. Aldolase B was predominantly found in adult liver, where aldolase A and C were distinctly low. Aldolase A and B showed almost the same concentration in fetal liver, while in neonatal liver aldolase B protein concentrations were much higher than aldolase A. In contrast, aldolase A was the predominant isozyme found in hepatoma and gastric cancer tissues, whereas aldolase B was distinctly low in hepatoma tissues, and extremely low in gastric cancer tissues. These results suggest that the aldolase A is a more fetal type of liver isozyme than the aldolase B and C, and aldolase B is a more differentiated type of liver isozyme than aldolase A and C. Serum FDP aldolase activities were elevated in half of patients with liver diseases, all patients with muscle diseases and a few patients with cancer. Serum aldolase A levels were elevated in patients with muscle diseases and cancer, but not elevated in patients with liver diseases. In contrast, serum aldolase B levels were elevated in patients with liver disease, but not elevated in patients with muscle diseases and other diseases without liver injury. Serum aldolase B levels showed a trend to decrease in cancer patients with normal GPT levels. Serum aldolase A/B ratios were significantly increased in cancer patients with normal GPT levels, whereas they showed the decreased levels in patients with liver diseases. These results suggest that measurement of aldolase isozymes by subunit specific radioimmunoassays may be useful in the diagnosis of certain cancers, myopathies and liver diseases. © 1994 Wiley‐Liss, Inc.
Genotype‐phenotype pitfalls in Gaucher disease
Authors: Strasberg Paula M. , Triggs‐Raine Barbara L. , Warren Irene B. , Skomorowski Marie‐Anne , McInnes Beth , Becker Laurence E. , Callahan John W. , Clarke Joe T. R. 
Published: March 2007

AbstractGaucher disease (GD), caused by inherited deficiency of β‐glucocerebrosidase (β‐Glc, EC 3.1.2.45), is classified type I if the CNS is not involved (non‐neuronopathic), type II if CNS involvement is early and rapidly progressive (acute neuronopathic), and type III if CNS involvement occurs later and is slowly progressive (subacute neuronopathic). The clinical course is not predictable by measurement of residual β‐Glc activity. Patient classification by identification of specific mutations is more promosing: homozygosity for the common A5841 ‐>(N370S) mutation invariably predicts type I; homozygosity for the T6433 ‐>C (L444P) mutation usually indicates type III (Norbottnian). Type II disease patients often carry the T6433 ‐>C allele together with a complex allele derived in part from the downstream pseudogene by crossover or gene conversion, producing a T6433 ‐>C substitution, plus 2 or 3 additional single base substitutions (fusion gene). Employing selective PCR amplification of the structural gene, we detected homozygous T6433C (L444P) point mutations in a Caucasian boy, initially classified as having GD type I, who succumbed to severe visceral GD before age 3 years. A second novel PCR procedure for discriminating between the normal gene and the fusion gene confirmed the homozygous point mutation results. Post mortem neuropathological findings showed neuronal complex lipid accumulation consistent with late‐onset type III disease. Although in Norbottnian patients it is generally accepted that onset of neurological findings is delayed, patients with the L444P/L444P genotype can only be initially classified as type Ill with this ancestry. Other patients described sporadically elsewhere are invariably considered type I until neurological findings arise. This is the first actual demonstration of a transition from type I to type Ill based on medical findings, not geography. © 1994 Wiley‐Liss, Inc.
Correlation of serum concentrations of psa‐act complex with total psa in random and serial specimens from patients with bph and prostate cancer
Authors: Wu James T. , Wilson Lorraine , Zhang Ping , Wayne Meikle A. , Stephenson Robert 
Published: March 2007

AbstractThe current assays for serum prostate specific antigen (PSA) have failed to produce the same PSA values on the same specimens because of problems with antibody specificity and calibrator preparation. To eliminate these problems, we proposed to replace the current serum PSA assay with an assay specific for the PSA‐ACT (PSA‐α1‐antichymotrypsin) complex in the serum. An assay specific for the PSA‐ACT complex was established using the anti‐PSA antibody to coat the microplate for capturing the PSA complex and anti‐ACT polyclonal antibodies for quantification. There was an excellent correlation between serum concentrations of PSA‐ACT and total PSA, using either the Hybritech calibrator (γ = 0.996) or a serum calibrator prepared in house (γ = 0.993), in random as well as in serial specimens from 14 individual patients. Even though we did not find a gradual increase in the percentage of PSA‐ACT with the increase of total PSA in cancer patients, a slightly higher percentage of free PSA was measured in pooled normal sera (18%) and in pooled sera containing only 12 ng/ml of total PSA (12%), compared to serum pools containing elevated PSA (>100 ng/ml) level, in which most PSA was in the complex form (95%). Therefore, using an assay that specifically measures the PSA‐ACT complex in the serum not only simplifies the preparation of calibrator but eliminates the difficulty of antibody selection, it also allows various assay kits to produce identical PSA values and also improve the test specificity for prostate cancer.©1995 Wiley‐Liss, Inc.
A novel magnetic particle agglutination in microtiter plates for rapid detection of human t‐lymphotropic virus type i antibody
Authors: Sohma K. , Kinoshita Y. , Morishita S. , Fujino R. , Saito T. 
Published: March 2007

AbstractWe have developed a novel magnetic particle agglutination (MPA) method for rapid detection of antibody to human T‐lymphotropic virus type I (HTLV‐I). This method is suitable for screening determination. The assay uses purified viral antigen coated on magnetic particles, which are novel artificial particles made of gelatin, arabic gum, and ferrite. MPA uses a special magnet and inclined plate holder. In MPA, the specimen is incubated with magnetic particles in the well; magnetic particles are then magnetically attracted to the bottom of the well. Then the plate is inclined and read by the naked eye. In a positive specimen, agglutination particles stay at the bottom of the well. On the other hand, non‐agglutination particles with negative sample run down the side of the well. The total assay time of MPA was estimated at 8 min/microtiter‐plate. The results obtained by correlating MPA for the detection of HTLV‐I antibody with other method emphasized the precision of MPA.©1995 wiley‐Liss, inc.