Purification and Some Properties of Dipeptidyl Carboxypeptidase from Bacillus pumilus(Biological Chemistry)

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概要

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• An intracellular protease from a bacterium, Bacillus pumilus HL721, was purified about 5000-fold by chromatography with a Q-Sepharose Fast Flow column, TSK-gel HA-1000 glass column, and TSK-gel G3000SWXL column using Bz-Gly-Ala-Pro as a substrate. The enzyme was the most active at pH around 7.5 and stable from 4.5 and 8.0. The enzyme activity was inhibited by Cu^<2+>, EDTA, N-ethylmaleimide, o-phenanthroline, and p-chloromercuribenzoic acid. The molecular weight of the enzyme was 155,000 by gel filtration. The enzyme removed dipeptide from the carboxyl end of some peptides used as substrates. From these results the enzyme seems to be a dipeptidyl carboxypeptidase.

• 社団法人日本農芸化学会の論文
• 1990-04-23

著者

• NAGAMORI YOICHI

  Ezaki Glico Biochemical Research Laboratories

• OKADA SHIGETAKA

  Ezaki Glico Biochemical Research Laboratories

• FUJISHIMA Noboru

  Ezaki Glico Biochemical Research Laboratories

• Nagamori Y

  Ezaki Glico Biochemical Research Laboratories

関連論文

• Isolation and Characterization of a Bacterial Dipeptidyl Carboxypeptidase Inhibitor from Bacillus subtilis 3-16-20
• Hydrolysis of Substance P and Related Compounds by Dipeptidyl Carboxypeptidase from Bacillus pumilus
• Enzymatic Properties of Dipeptidyl Carboxypeptidase from Bacillus pumilus(Biological Chemistry)
• Purification and Some Properties of Dipeptidyl Carboxypeptidase from Bacillus pumilus(Biological Chemistry)

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