ラツト肝臓リソソームに存在するアリルアミダーゼの精製と性質(自然科学編)

概要

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Rat liver lysosomes contain an arylamidase which has molecular weight of 135,000, and is separated into seven forms under isoelectric focusing. One form of these arylamidases, having isoelectric point of 7.8(form IV), was purified from rat liver by conventional chromatographic techniques. Final preparation of form VI appeared homogeneous by polyacrylamide disk electrophoresis and consisted of three identical polypeptide chain, as judged by disk electrophoresis in the presence of sodium dodecyl sulfate. The enzyme hydrolyzed naphthylamides of neutral amino acids but did not hydrolyze naphthylamides of basic, aromatic and acidic amino acids. The pH optimum for the hydrolysis of valine-β-naphthylamide was 7.0. The enzyme was inhibited by sulfhydryl-reactive reagents, TPCK, TLCK, and protease inhibitors of microbial origin, but not by puromycin. The enzyme hydrolyzed dipeptides and tripeptides. The pH optimum of the enzyme for the hydrolysis of Leu-Leu was 7.5. Physiological roles of the enzyme in lysosomes are discussed.
中村学園大学の論文
1992-02-28