Korean Journal of Microbiology (미생물학회지)
- Volume 24 Issue 2
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- Pages.119-126
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- 1986
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Isolation and properties of protease Pi in escherichia coli
대장균 세포내 단백질 분해효소, protease Pi의 정제와 특성
Abstract
A periplasmic endoprotease, named protease Pi, was purified to homogeneity from Escherkchia coli by conventional procedure with insulin as substrate. This enzyme degrades insulin and glucagon to trichloroacetic acid-soluble meterials, but shows little or no hydrolysis of bovine serum albumin, casein or globin. Its molecular weight was 110, 000 when determined by gel filtration on Sephacryl S-300 and was 105, 000 when estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Thus, it appears to be single polypeptide. This snzyme is metalloprotease, since it is completely inhibited by o-phenanthroline and can be activated by addition of divalent metal cations, such as