Judul: Studi Fenologi dan Distribusi Beberapa Jenis Rumput Dominan Pada Lansekap Lapangan Sepak Bola Senayan (Jakarta)
Abstrak: Tujuan percobaan ini adalah mengamati distribusi beberapa jenis rumput dominan padalansekap lapangan sepak bola Senayan (Jakarta) dan mengamati fenologi rumput. Distribusi beberapa jenis rumput dominan pada lansekap lapangan sepak bola Senayan (Jakarta) dianalisis dengan moetode Titik. Tiga spesies rumput yaitu Cynodon dactylon (L.) Pers, Zoysia matrella (L.) Merr dan Axonopus compressus (Swartz Beauv diamati fenologinta dengan rancangan acak kelompok. PErcobaan dilaksanakan di Lapangan Sepak Bola Stadion Utama Senayan (Jakarta) dan di Lapangan Sepak Bola ABC Senayan (Jakarta).
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Judul: Karakterisasi fisiologi rumput bermuda(Cynodon dactylon L.) lokal dalam rangka pengembangan turfgrass asli Indonesia
Abstrak: Penelitian ini dilaksanakan di Turfgrass Club IPB, Laboratorium RGCI (Research Group on Crop Development), dan Laboratorium Ekofisiologi Tanaman, Departemen Budidaya Pertanian, IPB pada bulan November 2004 sampai dengan bulan Mei 2005. Tujuan penelitian ini adalah untuk mendapatkan pertelaan karakter fisiologi rumput bermuda (Cynodon dactylon L.) lokal hasil koleksi dari beberapa daerah untuk pengembangan turfgrass asli Indonesia. Penelitian ini menggunakan Rancangan Kelompok Lengkap Teracak dengan satu faktor, yaitu rumput bermuda hasil koleksi yang berjumlah 45 aksesi. Rumput bermuda introduksi varietas Tifway dan Tifdwarf, serta rumput babat digunakan sebagai pembanding. Karakterisasi fisiologi dilakukan dengan 3 ulangan sehingga seluruhnya terdapat 144 satuan percobaan berupa pot berdiameter 30 cm. Karakterisasi fisiologi menghasilkan koefisien keragaman, dimana hanya karakter laju pertambahan bobot kering hasil pangkasan yang memiliki koefisien keragaman diatas 20%, sedangkan karakter lainnya menunjukkan koefisien keragaman dibawah 20%. Analisis gerombol menghasilkan dendogram dengan rentang koefisien ketidaksamaan antar aksesi sebesar 0-95%. Pemotongan dendogram dilakukan pada koefisien ketidaksamaan 62% dan menghasilkan 6 kelompok besar. Pada kelompok 6 terdapat aksesi yang memiliki kedekatan ciri fisiologi dengan rumput bermuda introduksi, yaitu: Cianjur 3, Jasinga 2, Jasinga 6, dan Pangalengan 6.
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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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