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Quantitation and significance of 125I-calmodulin binding to myosin light chain kinase and phosphorylase distributed on polyacrylamide gels.

Publication ,  Journal Article
Slaughter, GR; Means, AR
Published in: Biochem Biophys Res Commun
January 16, 1985

Glycogen phosphorylase (a or b) binds 125I-calmodulin in a Ca2+-dependent manner, in the 125I-calmodulin overlay technique. This binding is quantitatively identical to 125I-calmodulin binding to myosin light chain kinase. In an in vitro assay, calmodulin stimulates phosphorylase activity at limiting concentrations of either glucose-1-phosphate or glycogen, but the Ka is 1000 fold higher than for the kinase, and is not Ca2+-dependent. Activation of phosphorylase, but not myosin light chain kinase, by calmodulin can be mimicked by troponin C or bovine serum albumin. These results demonstrate that the properties of calmodulin interaction with proteins can vary between the 125I-calmodulin technique and a functional assay of calmodulin effect on the same protein.

Duke Scholars

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

January 16, 1985

Volume

126

Issue

1

Start / End Page

295 / 303

Location

United States

Related Subject Headings

  • Rabbits
  • Protein Kinases
  • Phosphorylases
  • Phosphorylase b
  • Phosphorylase a
  • Myosin-Light-Chain Kinase
  • Molecular Weight
  • Liver
  • Kinetics
  • Enzyme Activation
 

Citation

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Slaughter, G. R., & Means, A. R. (1985). Quantitation and significance of 125I-calmodulin binding to myosin light chain kinase and phosphorylase distributed on polyacrylamide gels. Biochem Biophys Res Commun, 126(1), 295–303. https://doi.org/10.1016/0006-291x(85)90605-9
Slaughter, G. R., and A. R. Means. “Quantitation and significance of 125I-calmodulin binding to myosin light chain kinase and phosphorylase distributed on polyacrylamide gels.Biochem Biophys Res Commun 126, no. 1 (January 16, 1985): 295–303. https://doi.org/10.1016/0006-291x(85)90605-9.
Slaughter, G. R., and A. R. Means. “Quantitation and significance of 125I-calmodulin binding to myosin light chain kinase and phosphorylase distributed on polyacrylamide gels.Biochem Biophys Res Commun, vol. 126, no. 1, Jan. 1985, pp. 295–303. Pubmed, doi:10.1016/0006-291x(85)90605-9.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

January 16, 1985

Volume

126

Issue

1

Start / End Page

295 / 303

Location

United States

Related Subject Headings

  • Rabbits
  • Protein Kinases
  • Phosphorylases
  • Phosphorylase b
  • Phosphorylase a
  • Myosin-Light-Chain Kinase
  • Molecular Weight
  • Liver
  • Kinetics
  • Enzyme Activation