DETAIL JURNAL
UMUL KARIMAH, SONY HERU SUMARSONO
Vol.10 No.1 April 2017
Program Studi Farmasi, Universitas Nahdlatul Ulama Kalimantan Timur, Program Studi Bioteknologi, Laboratorium Fisiologi Perkembangan Hewan dan Sains Biomedika, Sekolah Ilmu dan Teknologi Hayati (SITH)
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Protein isolation is the primary step in protein investigation. Methods for isolating protein
depend on protein solubility, size, charge and affinity. Immunoglobulin Y (IgY) is the major
antibody in avian immune system and presents in high amount in egg yolk. Its transfer from hen
blood to the egg yolk requires specific receptor which is long predicted as a membrane protein of
granulosa cells. This research aimed to isolate the putative receptor of IgY from membrane protein
of granulosa cells with affinity purification method. Pure IgY was immobilized to CNBr-activated
Sepharose 4B matrix as affinity ligand. Membrane proteome of granulosa cells from F1-F3
follicles was incubated in this affinity matrix with PBS pH 8,0. Fraction eluted with PBS pH 6,0
was examined with SDS-PAGE in reducing condition and showed 68 kDa band with very high
intensity. This 68 kDa protein is putative receptor of IgY in granulosa cells membrane.
Keywords: affinity; granulosa cells; immunoglobulin Y; receptor.
