Partial purification and some properties of a benzhydrylamide-bond hydrolyzing enzyme in Pseudomonas diminuta.

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概要

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• An enzyme in Pseudomonas diminuta showed hydrolyzing activity of a benzhydrylamide (=diphenylmethylamide) bond in S-benzylcysteinylglycine benzhydrylamide. The enzyme was purified 225-fold by precipitation with ammoniumsulfate, and column chromatography with ECTEOLA-cellulose, DEAE-cellulose and hydroxyapatite. It showed an optimum pH of 6 to 8 and it was markedly inhibited by Hg2+ or p-chloromercuribenzoate. The preparation was more specific against S-benzylcysteinylglycine benzhydrylamide than other substrates tested.

• 公益社団法人 日本農芸化学会の論文

著者

• HAYASHI Mineyuki

  Tokyo Research Laboratory, Kyowa Hahko Kogyo Co.

関連論文

• Partial purification and some properties of a benzhydrylamide-bond hydrolyzing enzyme in Pseudomonas diminuta.

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