A Succinyl-trialanine p-Nitroanilide Hydrolase in Hog Kidney Cytosol : Its Identification as Proline Endopeptidase

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概要

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• A succinyl-trialanine p-nitroanilide [Suc-(Ala)_3-pNA] hydrolase which is able to hydrolyze an artificial elastase substrate, Suc-(Ala)_3-pNA, but unable to hydrolyze a naturally occurring substrate, elastin, was highly purified from hog kidney cytosol. The apparent molecular weight of the enzyme was estimated to be 65000 by gel filtration on Sephadex G-150 and 68000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the isoelectric point of the enzyme was 5.0. The enzyme is an endopeptidase which catalyzes the hydrolysis of peptides with the general structure Y-Ala (or Pro)-X (Y=peptide or N-protected amino acid ; X=amino acid moiety, peptide or amide) at the carboxyl side of alanine and proline residues. The enzyme was markedly inhibited by diisopropyl fluorophosphate and p-chloromercuribenzoate. Ethylenediaminetetraacetate and 1,10-phenanthroline, however, were not inhibitors of the enzyme. The enzyme activity was retained on an affinity column having a proline endopeptidase [EC 3.4.21.26] inhibitor, Z-Gly-Pro, as ligand and could be eluted at 0.125M NaCl (mean value). Suc-(Ala)_3-pNA-hydrolytic activity coincided with the peak of proline endopeptidase activity as determined with a sensitive fluorogenic substrate, succinylglycyl-L-proline 4-methylcoumaryl-7-amide (Suc-Gly-Pro-MCA). The optimum pH and k_<cat>/K_m values (mM^<-1>・s^<-1>) were pH 7.5 and 5.4 for Suc-(Ala)_3-pNA and pH 6.8 and 24.8 for Suc-Gly-Pro-MCA, and the enzyme activity was competitively inhibited by Z-Ala-Ala and Z-Gly-Pro, as is the case with proline endopeptidase. These results suggest that Suc-(Ala)_3-pNA hydrolase in hog kidney cytosol may be identical with proline endopeptidase which was first found in human uterus as an oxytocindegrading enzyme.

• 公益社団法人日本薬学会の論文
• 1984-04-25

著者

• 永松 淳雄

  Faculty of Pharmaceutical Sciences, Fukuoka University

• 永松 淳雄

  福岡大学薬学部

• 添田 秦司

  Faculty of Pharmaceutical Sciences, Fukuoka University

• 永松 淳雄

  Faculty Of Pharmaceutical Sciences Fukuoka University

• 大山 政則

  Faculty of Pharmaceutical Sciences, Fukuoka University

• 添田 秦司

  Faculty Of Pharmaceutical Sciences Fukuoka University

• 添田 秦司

  福岡大学 薬

• 大山 政則

  Faculty Of Pharmaceutical Sciences Fukuoka University

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