Purification of Arginase from Goat Liver Tissue

Abstract

       The study aimed to purification of Arginase from goat liver tissue, this study included extraction enzyme from local goat liver tissue. The purification process was done with several steps included homogenized crude extract, heat treatment, precipitation with inorganic salt (NH4) ₂SO4 30%-70%, ion exchange chromatography by DEAE Sepharose anion column, and size exclusion chromatography by Sepharose 6B. Consequences have depicted a precipitate and concentrated protein with six peaks in ion exchange column. arginase positioned in the first and fourth peak with purification  fold (3.8, 3.2) , yield (3.2 ,3.4)) of enzyme and specific activity (99.18 ,82.5)) IU/ml respectively, which  obtained a single peak  by gel filtration chromatography from isoenzyme I, the degree of purification (8.06) fold, yield of enzyme (4.7) with specific activity (210.7) IU/ml, also, the peak that has the highest enzymatic activity showed single peak after elution in gel filtration chromatography following steps based on SDS- PAGE Electrophoresis .From this paper, it is concluded that arginase purified from goat liver tissue  has two  isoenzymes with molar mass about 48,000 (±1000)  Daltons. Also, it has concluded that purity and molar mass of purify arginase have shown approximately ~ 46 KD with single band by gel filtration chromatography.