Analysis and Partial Purification of Heat Stable Proteins in Sheep Liver Homogenate by Salt Fractionation Using Ammonium Sulfate
Aara Rifat, S. A. Hajam and K. I. AndrabiDepartment of Biochemistry, University of Kashmir, Kashmir -190 006 (India).
Abstract: Heat stability refers to the fraction of proteins that remain soluble when heated to 90°C thus greatly facilitating their enrichment subsequent purification. Under these conditions approximately 95% of the total cell protein (heat stable) fraction from sheep liver homogenate was thus prepared and analyzed to meet the objectives of the study.The thermolabile proteins were removed by centrifugation and supernatant containing soluble proteins were stored until processed further. At least proteins were purified to homogeneity using conventional biochemical techniques of salt fractionation with ammonium sulfate, followed by DEAE-Cellulose chromatography and the purity analyzed by SDS-page.
Keywords: HSP Salt fractionation; SDSpage Back to TOC