Isolation and properties of protease Pi in escherichia coli

대장균 세포내 단백질 분해효소, protease Pi의 정제와 특성

  • 이영섭 (서울대학교 자연과학대학 동물학과) ;
  • 곽태환 (서울대학교 자연과학대학 동물학과) ;
  • 임정빈 (서울대학교 미생물학과) ;
  • 정진하 (서울대학교 자연과학대학 동물학과)
  • Published : 1986.06.01

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 $Mg^{2+}\;and\;Co^{2+}$. It is destinct from protease Ci, a cytoplasmic insulin degrading enzyme, since protease Pi is localized to the periplasm. Since protease Pi selectively degrades GTP cyclohydrolase I, it appears to play a role in the regulation of pteridine biosynthesis.

Keywords

periplasmic endoprotease;E.coli