Abstract
Arginase from rat liver was separable into two isozymes (Isozyme-I and -II). These two isozymes were purified and their properties were studied. The purification procedure was composed of homogenization, heat treatment, acetone precipitation, ethanol fractionation, CM-Sepharose chromatography, isoelectric focusing, and Sephadex G-200 gel filtration.The purified preparation of Isozyme-I and -II were respectively homogeneous in polyacrylamide gel electrophoresis. These two isozymes were similar to each other with respect to the Km for L-arginine and the Ki's for the competitive inhibitors, L-ornithine and L-lysine. Their optimal pHs were in the range of 10.3-10.5. There was no immunological difference between the isozymes. The isoelectric points of Isozyme-I and -II were 9.3 and 9.5, respectively. All the subunits of both isozymes had a molecular weight of 40, 000 in SDS-polyacrylamide gel electrophoresis. The results of the analysis of N-terminal amino acids suggest that both isozymes are composed of different kinds of subunits.
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