Purification and properties of caldesmon-like protein from molluscan smooth muscle

Comp Biochem Physiol Biochem Mol Biol. 1994 May;108(1):59-63. doi: 10.1016/0305-0491(94)90165-1.

Abstract

In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calmodulin-Binding Proteins / chemistry
  • Calmodulin-Binding Proteins / genetics
  • Calmodulin-Binding Proteins / isolation & purification*
  • Chickens
  • Cloning, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Mollusca / chemistry*
  • Mollusca / genetics
  • Muscle Proteins / chemistry
  • Muscle Proteins / genetics
  • Muscle Proteins / isolation & purification
  • Muscle, Smooth / chemistry
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Calmodulin-Binding Proteins
  • Muscle Proteins