Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin

Pascal J. Goldschmidt-Clermont, Robert C. Allen, Andre E. Nel, David L. Emerson, Joseph R. Day, Robert M. Galbraith

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Limited proteolysis of G-actin was performed with trypsin and chymotrypsin to compare the binding sites for Gc and DNase. DNase I bound to the N-terminal area corresponding to the major cleavage site on G-actin (residues 62-68) and inhibited proteolysis, but did not bind the 33.5K C-terminal fragment (G-actin33.5) generated. In contrast, Gc did not exert any inhibitory effect upon proteolysis of the intact native G-actin42.0 molecule, although its presence protected G-actin33.5 from further proteolysis. This was shown by gel filtration to be due to the formation of complexes between Gc and G-actin33.5.

Original languageEnglish (US)
Pages (from-to)735-742
Number of pages8
JournalLife Sciences
Volume38
Issue number8
DOIs
StatePublished - Feb 24 1986

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

Fingerprint Dive into the research topics of 'Gc (vitamin D-binding protein) binds the 33.5 K tryptic fragment of actin'. Together they form a unique fingerprint.

Cite this