Purification and characterization of a protein inhibitor of calcium-dependent proteases from rat liver

George N. Demartino, Dorothy E. Croall

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Soluble extracts of rat liver contain a protein inhibitor of calcium-dependent proteases. The inhibitor has an apparent Mr = 250,000 and is separated from the calcium-dependent proteases by gel-filtration chromatography in the presence of EGTA. The inhibitor has been purified by affinity chromatography using a calcium-dependent protease covalently linked to Affi-Gel 15. The inhibitor specifically binds to this affinity resin in a calcium-dependent manner and elutes in the presence of EDTA or EGTA. The purified inhibitor appears as a single protein with Mr = 125,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Presumably it is a dimer under nondenaturing conditions. The inhibitor inhibits each of two calcium-dependent proteases from rat liver and from other tissues and species. However, it has no effect on any other protease tested.

Original languageEnglish (US)
Pages (from-to)713-720
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume232
Issue number2
DOIs
StatePublished - Aug 1 1984

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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