Judul: Pemetaan Tanah Detil Kebun Percobaan Leuwikopo-Institut Perlanian Bogor, Bogor
Abstrak: Penelitian dilakukan di Kebun Percobaan milik Fakultas Politeknik Pertanian, Institut Pertanian Bogor yang terletak di Kampung Leuwikopo, Desa Babakan, Kecamatan Ciomas, Kabupaten Bogor. Pelaksanaan peneli tian dilakukan dalam 2 tahap, yaitu: di lapangan dari mulai Mei sampai Juli 1985, dan di laboratorium dari bulan Juli sampai September 1985.
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Judul: Pemetaan Tanah Detail dan Evaluasi Kesesuaian Lahan Kebun Percobaan Fakultas Pertanian Institut Pertanian Bogor Darmaga
Abstrak: Tujuan penelitian ini adalah mempelajari sifat-sifat tanah yang ada di daerah penelitian, mengklasifikasikannya sampai kategori famili dengan menggunakan Kunci Taksonomi Tanah (Soil Survey Staff, 1998), mengelompokkan dan membatasi tanah yang mempunyai sifat yang sama kedalam satuan peta tanah tersendiri dan menyajikannya dalam bentuk peta tanah detail. Disamping itu dilakukan evaluasi kesesuaia lahan untuk tanaman pangan lahan kering dan tahunan, sehingga diharapkan hasil penelitian ini dapat digunakan sebagai bahan pertimbangan dalam melaksanakan percobaan lapangan ditempat lain.
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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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