Judul: Revisi marga Anadendrum schott (Araceae) di Malesia
Abstrak: Anadendrum merupakan tumbuhan terna memanjat dari suku talas-talasan (Araceae) yang mempunyai nilai ekonomi penting bagi manusia. Dalam taksonominya, tumbuhan ini masih ada beberapa kerancuan yang dapat membingungkan pemakainya. Untuk itu maka perlu dilakukan revisi marga maupun jenisnya, sehingga taksonomi tumbuhan marga Anaden- drum menjadi lebih mantap dan benar. Penelitian bertujuan untuk merevisi marga Anadendrum dan jenisnya yang ada di Malesia dengan pendekatan secara morfologi dan anatomi daun. Disamping itu juga untuk mengetahui kekerabatan antar jenis-jenisnya. Penelitian dilakukan pada bulan Juli 1993 sampai Nopember 1994 di Herbarium Bogoriense. Pengamatan morfologi dan anatomi dilakukan pada spesimen-spesimen herbarium yang berasal dari Bogor, Singapura dan Leiden. Pengamatan ciri morfologi dengan melihat bagian-bagian akar, batang,..dst
Keyword: Talas-talasan, Nilai ekonomi, Herbarium Bogoriense, Bogor

Judul: Revisi marga chealomappa (Euphorbiaceae) di kawasan Malesia
Abstrak: Marga Cephalomappa Baillon di kawasan Malesia direvisi berdasarkan ciri-ciri morfologi dan anatomi dengan menggunakan koleksi-koleksi spesimen yang tersedia di Herbarium Bogoriense dan spesimen yang dipinjam dari Kew herbarium, Leiden Rijks- herbarium, London The Natural History Museum-British Museum dan Singapore Herbarium. Studi yang disajikan ini didasarkan pada pengamatan 135 koleksi spesimen spesimen yang tersedia tersebut, 5 (lima) jenis Cephalomappa diakui identitasnya berada di kawasan Malesia, yaitu C. beccariana, C. lepidotula, C malloticarpa, C. paludicola, C. penangensis dan empat varietas dari C. beccariana. Pertelaan jenis berikut persebarannya, nama daerah, ekologi, kunci identifikasi jenis dan varietasnya demikian pula gambar dan indeks dari semua spesimen yang diuji akan disajikan. Analisis Kladistika dengan menggunakan program Hennig86 yang didasarkan pada data morfologi memperlihatkan, bahwa C. beccariana, C. lepidotula dan C. penangensis sangat berkerabat dekat. Dan dalam kladogram memperlihatkan satu sister group dari C. beccariana, pada cabang terakhir.
Keyword: Marga Cephalomappa Baillon, Herbarium Bogoriense, Analisis Kladistika

Judul: Pemurnian dan karakterisasi protein inhibitor RNA helikase virus hepatitis C
Abstrak: Hepatitis C virus (HCV) infection is the second most common chronic viral infection in the world with global prevalence. This infection is contribution to chronic hepatitis and liver cirrhosis, often leading to hepatocellular carcinoma. There is no effective drug and vaccine available against HCV. The current standard treatment, a combination of pegylated interferon-α with ribavirin, is limited by its suboptimal response rate in a significant patient population, side effects, and affordability. Therefore, development of effective drug is needed. One approach to find out the candidate of antiviral drug is to discover the inhibitor of enzyme that essential for virus replication, such as RNA helicase. Streptomyces chartreusis 5-095 produce the inhibitor of HCV RNA helicase. The aim of this study was to purify the protein inhibitor which has inhibition activity against ATPase activity of RNA helicase HCV from S. chartreusis 5-095. The supernatant of culture S. chartreusis 5-095 exhibited high inhibiton activity against ATPase activity of RNA helicase HCV (approximately 72%) at 10 days of incubation. The extracellular protein inhibitor was partially purified by procedures of precipitation with ammonium sulfate to 65% saturation and gel filtration (Sephadex G50) using methanol water solution (4:6) as an eluen. The purity of protein inhibitor was monitored by SDS PAGE. The protein inhibitor showed a relative molecular mass were estimated to be 14 kDa and increased the purity 23,08 fold than those of the crude protein. The specific activity and IC50 after purification were 13,1338 U/mg and 0,0767 mg/mL, respectively. The activity of purified protein inhibitor showed its stability over pH range from 5-8 and optimum at pH 7,4. The inhibition activity showed its stability up to 70% at temperature 100 oC. The purified protein inhibitor relatively stable its activity at storage in the range of -20 oC to room temperature for 35 days.
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