A simple and rapid preparation of fully phosphorylated and fully dephosphorylated skeletal muscle myosin. Application to the preparation of a phosphorylated LC2-modified artificial isozyme-Reference-Cited by-同舟云学术

A simple and rapid preparation of fully phosphorylated and fully dephosphorylated skeletal muscle myosin. Application to the preparation of a phosphorylated LC2-modified artificial isozyme

Published:1986-10 Issue:5 Volume:7 Page:455-466
ISSN:0142-4319
Container-title:Journal of Muscle Research and Cell Motility
language:en
Short-container-title:J Muscle Res Cell Motil

Author:

Cardinaud R.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry,Physiology

Link

http://link.springer.com/content/pdf/10.1007/BF01753588.pdf

Reference32 articles.

1. Bagshaw, C. R. &Kendrick-Jones, J. (1979) Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosin using electron paramagnetic resonance spectroscopy.J. molec. Biol. 130, 317–36.

2. Bailey, J. L. (1967) Estimation of Proteins. InTechniques in Protein Chemistry, pp. 340–52. Amsterdam: Elsevier Publishing Company.

3. Bárány, K., Vander Meulen, D. L., Ledvora, R. F. &Bárány, M. (1982) Selective phosphorylation of myosin light chain in intact skeletal muscle.Archs Biochem. Biophys. 217, 392–6.

4. Blumenthal, D. K. &Stull, J. T. (1980) Activation of skeletal muscle myosin light chain kinase by calcium (2+) and calmodulin.Biochemistry 19, 5608–14.

5. Cardinaud, R. (1980) Fate of the light chains in the course of proteolytic digestion of rabbit fast skeletal myosin.Biochimie 62, 135–45.

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