Retno D Soejoedono
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KONSENTRASI PROTEIN DAN PENENTUAN BERAT MOLEKUL EKSKRETORI/SEKRETORI L3 Ascaridia galli D, Darmawi; Balqis, Ummu; Tiuria, Risa; Soejoedono, Retno D; Pasaribu, Fachriyan H
Jurnal Kedokteran Hewan Vol 3, No 1 (2009): J. Ked. Hewan
Publisher : Syiah Kuala University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (863.975 KB) | DOI: 10.21157/j.ked.hewan.v3i1.3074

Abstract

Penelitian ini bertujuan menentukan konsentrasi dan berat molekul protein  ekskretori/sekretori larva (L3) Ascaridia galli (A. galli). Larva L3 diperoleh dari usus halus 100  ayam tujuh hari setelah pemberian dosis 6000 L2 melalui esofagus ayam. Sebanyak 5–10  L3 dikultur secara in vitro  dalam setiap ml medium Rosswell Park Memorial Institute (RPMI 1640), pH 6,8, tanpa merah fenol dalam inkubator pada temperatur 37 0C dan 5% CO2 selama 3 hari. Ke dalam medium ditambahkan 100 unit ml-1 penisilin G, 100 µg ml-1 streptomisin, 5 µg ml-1 gentamisin dan 0,25 µg ml-1 kanamisin. Ekskretori/sekretori dipreparasi dari produk metabolisme L3 yang dilepaskan ke dalam medium kultur. Untuk mendapatkan protein ekskretori/sekretori, medium kultur dipekatkan dengan vivaspin 30.000 MWCO, dan kuantitas protein dihitung dengan metode Bradford. Berat molekul protein ekskretori/sekretori divisualisasikan dengan sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Hasil penelitian  menunjukkan bahwa konsentrasi protein ekskretori/sekretori adalah 0,595 mg/ml dengan berat molekul 28 kDa.
Molecular analysis of Hemagglutinin Gen of Highly Pathogenic Avian Influenza of H5N1 Subtype Isolated from Waterfowls Susanti, R; Soejoedono, Retno D; K Mahardika, I Gusti Ngurah; T Wibawan, I Wayan; Suhartono, Maggy T
Indonesian Journal of Animal and Veterinary Sciences Vol 13, No 3 (2008)
Publisher : Indonesian Animal Sciences Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (423.147 KB) | DOI: 10.14334/jitv.v13i3.584

Abstract

Avian influenza viruses (AIV) subtype H5N1 isolated from waterfowls in West Java pose the known characteristic of highly pathogenic strains, with polybasic amino acid sequence of cleavage site QRERRRKKR and QRESRRKKR. This research aimed to analyze the important domains of hemagglutinin (HA) gene of those isolates. Fragment of HA gene was amplified using RT-PCR method with specifically-designed primer pairs and sequenced using dideoxy termination method with ABI automatic sequencer (Applied Biosystems). Multiple alignment of nucleotide and deduced amino acid sequences were analyzed using ClustalW of MEGA-3.1 program. Some of biological domains of HA, i.e. antigenic sites, receptor binding pocket, and glycosylation sites of the isolates were polymorphic. The viruses also pose conserved glutamine (Q) and glisin (G) residues at the known receptor binding site, at the position 222 and 224 respectively. This findings clearly show that all AIV subtype H5N1 isolaed from waterfowl preservesthe α-2,3NeuAcGal avian receptor specificity. Key Words: Antigenic Sites, Glycosylation Sites, Receptor Binding Pocket, AIV H5N1, Waterfowls
Molecular analysis of Hemagglutinin Gen of Highly Pathogenic Avian Influenza of H5N1 Subtype Isolated from Waterfowls Susanti, R; Soejoedono, Retno D; K Mahardika, I Gusti Ngurah; T Wibawan, I Wayan; Suhartono, Maggy T
Jurnal Ilmu Ternak dan Veteriner Vol 13, No 3 (2008): SEPTEMBER 2008
Publisher : Indonesian Animal Sciences Society

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (423.147 KB) | DOI: 10.14334/jitv.v13i3.584

Abstract

Avian influenza viruses (AIV) subtype H5N1 isolated from waterfowls in West Java pose the known characteristic of highly pathogenic strains, with polybasic amino acid sequence of cleavage site QRERRRKKR and QRESRRKKR. This research aimed to analyze the important domains of hemagglutinin (HA) gene of those isolates. Fragment of HA gene was amplified using RT-PCR method with specifically-designed primer pairs and sequenced using dideoxy termination method with ABI automatic sequencer (Applied Biosystems). Multiple alignment of nucleotide and deduced amino acid sequences were analyzed using ClustalW of MEGA-3.1 program. Some of biological domains of HA, i.e. antigenic sites, receptor binding pocket, and glycosylation sites of the isolates were polymorphic. The viruses also pose conserved glutamine (Q) and glisin (G) residues at the known receptor binding site, at the position 222 and 224 respectively. This findings clearly show that all AIV subtype H5N1 isolaed from waterfowl preservesthe α-2,3NeuAcGal avian receptor specificity. Key Words: Antigenic Sites, Glycosylation Sites, Receptor Binding Pocket, AIV H5N1, Waterfowls
Molecular analysis of Hemagglutinin Gen of Highly Pathogenic Avian Influenza of H5N1 Subtype Isolated from Waterfowls Susanti, R; Soejoedono, Retno D; K Mahardika, I Gusti Ngurah; T Wibawan, I Wayan; Suhartono, Maggy T
Jurnal Ilmu Ternak dan Veteriner Vol 13, No 3 (2008): SEPTEMBER 2008
Publisher : Indonesian Center for Animal Research and Development (ICARD)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (423.147 KB) | DOI: 10.14334/jitv.v13i3.584

Abstract

Avian influenza viruses (AIV) subtype H5N1 isolated from waterfowls in West Java pose the known characteristic of highly pathogenic strains, with polybasic amino acid sequence of cleavage site QRERRRKKR and QRESRRKKR. This research aimed to analyze the important domains of hemagglutinin (HA) gene of those isolates. Fragment of HA gene was amplified using RT-PCR method with specifically-designed primer pairs and sequenced using dideoxy termination method with ABI automatic sequencer (Applied Biosystems). Multiple alignment of nucleotide and deduced amino acid sequences were analyzed using ClustalW of MEGA-3.1 program. Some of biological domains of HA, i.e. antigenic sites, receptor binding pocket, and glycosylation sites of the isolates were polymorphic. The viruses also pose conserved glutamine (Q) and glisin (G) residues at the known receptor binding site, at the position 222 and 224 respectively. This findings clearly show that all AIV subtype H5N1 isolaed from waterfowl preservesthe α-2,3NeuAcGal avian receptor specificity. Key Words: Antigenic Sites, Glycosylation Sites, Receptor Binding Pocket, AIV H5N1, Waterfowls
Preparasi Imunoglobulin Yolk (IgY) Spesifik Virus Rabies untuk Pengembangan Kit Diagnostik Ruhi, Suwarny; Murtini, Sri; Poetri, Okti Nadia; Soejoedono, Retno D
Acta VETERINARIA Indonesiana Vol 6, No 1 (2018): Januari 2018
Publisher : Bogor Agricultural University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29244/avi.6.1.30-37

Abstract

Penelitian ini bertujuan untuk memproduksi dan mengkarakterisasi IgY anti rabies sebagai bahan diagnostik. Ayam petelur usia produktif divaksinasi dengan vaksin rabies inaktif secara parenteral melalui rute intramuskular dengan dosis 0,5 ml sebanyak 2 kali. Keberadaan IgY pada telur dievaluasi dengan metode ELISA. Konsentrasi total protein IgY di hitung dengan metode Bradford. IgY dipurifikasi menggunakan dua metode yaitu : 1) pengendapan dengan NaCl, PEG 6000-amonium sulfat; 2) teknik Water Soluble Fraction (WSF), dilanjutkan pengendapan dengan PEG 6000-amonium sulfat.  Titer IgY spesifik  di tentukan dengan uji ELISA dan karakterisasi protein dengan metode SDS-PAGE. Hasil pengujian menunjukkan, antibodi anti-rabies dapat dideteksi pada kuning telur di minggu kedua setelah vaksinasi pertama. Purifikasi IgY dengan NaCl menghasilkan konsentrasi 331 µg/ml dan teknik WSF 184 µg/ml. Karakterisasi protein pada teknik NaCl menghasilkan 6 pita protein dengan berat molekul 164,16 kDa, 126,43 kDa, 97,36 kDa, 68,73 kDa, 40,76 kDa, 28,77 kDa sedangkan teknik WSF hanya terdiri dari 3 pita dengan berat molekul 94,03 kDa, 65,61 kDa, dan 31,94 kDa. Titer antibodi spesifik menggunakan teknik NaCl  lebih besar dari 0,5 IU/ml dan teknik WSF dengan titer antibodi di bawah 0,5 IU/ml . Berdasarkan hasil penelitian, dapat disimpulkan bahwa IgY spesifik rabies dapat diproduksi pada ayam petelur dan menghasilkan titer antibodi ? 0,5 IU/ml, dengan titer antibodi spesifik rabies sebesar ? 0,5 IU/ml.
PRODUKSI ANTIBODI KUNING TELUR (IgY) ANTI STREPTOCOCCUS MUTANS SEBAGAI ANTI KARIES GIGI Poetri, Okti Nadia; Soejoedono, Retno D
Jurnal Ilmu Pertanian Indonesia Vol 11, No 3 (2006): Jurnal Ilmu Pertanian Indonesia
Publisher : Institut Pertanian Bogor

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

The aim of this study was to explore IgY anti Streptococcus mutan production and the ability of Igy Streptococcus mutans blocking adhesion process. The eggs was collected from Single Comb Brown Leghorn which have been immunized by S. mutan. Agar gel precipitation test was done to detect IgY anti S. mutans in serum and egg. Egg which Countain IgY anti S. mutans was collected. IgY anti S. mutans extracted from egg yolk by mean s PEG-Amonium sulfat and purified using fast protein liquid chromatography. The purity of Igy anti S. mutans was determined by UV spectropometer. Biological activities of Igy anti S. mutans to inhibit adhession process was learned by anti adhesion test. We use two dose of IgY, which is 100 ug and 500 ug. Igy anti S.  mutans formen in serum  five weeks after the first immunization while it formed in egg nine weeks after the first immunization. Igy anti S. mutanss still present in serum andegg until twelve weeks from the first immunization. Igy anti S. mutanss  could decrease the amount of bacteria which attach the epithelial cell surface. The amount of sticky bacteria on epithelial cell (without IgY) are 40 cell bacteria/epithelial cell. After blocked by IgY anti S. mutanss  the amount of bacteria turn into 30 cell bacteria/epithelial cell (for dose of 100 ug IgY) and 28 cell bacteria/epitheelial cell (for dose of 500 ug IgY). This research concluded that hens were capable producing IgY anti S. mutanss in egg yolk and it can be used to solve dental caries problem which caused by S. mutanss.