A Rapid and Simple Method for Purification of the Chloride-Activated Arginine Aminopeptidase from Biological Materials |
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Authors: | Eva Söderling |
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Affiliation: | Department of Biochemistry , Institute of Dentistry, University of Turku , Turku, Finland |
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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 amino-acyl-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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Keywords: | Fermentation Acid hydrolyzate Sawdust Furfural 5‐Hydroxymethylfurfural (HMF) Anion exchange resin |
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