Abstract
A homogenous, chloride-dependent arginine amino-peptidase was purified from the liver of human fetuses by gel-permeation chromatography followed by subsequent fractionation on DEAE-Sepharose CL-6B and affinity chromatography on Sepharose 4B covalently coupled to L-arginine. The purified enzyme showed a single band on disc-gel electrophoresis. In SDS-gel electrophoresis the molecular weight of the enzyme was found to be 92'000 +/- 2000. N-L-Arginyl-2-naphthylamine and N-L-lysyl-2-naphthylamine were practically the only aminoacyl-2-naphthylamines hydrolyzed by the enzyme. The method was successfully applied for the purification of the chloride-dependent arginine aminopeptidases from human erythrocytes, serum, synovial fluid and rat inflammatory exudates.
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