Inhibition of calcium-dependent actin gelation by actin-binding protein from platelets

Biochem Int. 1990 Aug;21(5):823-30.

Abstract

Various proteins related to cell contraction have been extracted from human platelets. Of these, a protein (48K) with the molecular weight of 48,000 and one with the molecular weight of 47,000 (P47) often migrate together with actin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. We studied the biochemical characteristics of the 48K protein, purified by actin affinity and DEAE-Sepharose chromatography. The 48K protein did not react with anti-actin antibody or peroxidase-labelled actin. The protein inhibited the calcium-dependent gelation of actin. The 48K protein seemed to be a regulatory protein involving cell contraction not identified before.

MeSH terms

  • Actins / chemistry*
  • Actins / immunology
  • Blood Platelets / metabolism*
  • Calcium / metabolism*
  • Chromatography, Affinity
  • Gels
  • Humans
  • Microfilament Proteins / metabolism
  • Microfilament Proteins / pharmacology*
  • Molecular Weight

Substances

  • Actins
  • Gels
  • Microfilament Proteins
  • Calcium