Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle

Biochem Biophys Res Commun. 1986 Nov 26;141(1):20-6. doi: 10.1016/s0006-291x(86)80328-x.

Abstract

We isolated a 34,000-dalton protein from the heat-soluble fraction of avian smooth muscle using the procedures of ammonium sulfate fractionation, cation exchange chromatography and gel filtration. The amount of 34,000-dalton protein in the muscle homogenate was as much as tropomyosin. The 34,000-dalton protein bound to F-actin and F-actin-tropomyosin in a Ca2+-independent manner, but it Ca2+-dependently interacted with calmodulin. We tentatively named the 34,000-dalton protein gizzard p34K.

MeSH terms

  • Actins / metabolism
  • Animals
  • Calmodulin / metabolism
  • Calmodulin-Binding Proteins / isolation & purification*
  • Calmodulin-Binding Proteins / metabolism
  • Carrier Proteins / isolation & purification*
  • Carrier Proteins / metabolism
  • Gelsolin
  • Gizzard, Non-avian / analysis*
  • Isoelectric Point
  • Microfilament Proteins*
  • Molecular Weight
  • Muscle Proteins / isolation & purification*
  • Muscle, Smooth / analysis*
  • Protein Binding
  • Tropomyosin / metabolism

Substances

  • Actins
  • Calmodulin
  • Calmodulin-Binding Proteins
  • Carrier Proteins
  • Gelsolin
  • Microfilament Proteins
  • Muscle Proteins
  • Tropomyosin
  • brevin
  • gizzard p34K protein, chicken