Effects of phosphorylation, MgATP, and ionic strength on the rates of papain degradation of heavy and light chains of smooth muscle heavy meromyosin at the S1-S2 junction.-Reference-Cited by-同舟云学术

Effects of phosphorylation, MgATP, and ionic strength on the rates of papain degradation of heavy and light chains of smooth muscle heavy meromyosin at the S1-S2 junction.

Published:1988-08 Issue:22 Volume:263 Page:10974-10979
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Suzuki H,Kondo Y,Carlos A D,Seidel J C

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Structure and Function of Chicken Gizzard Myosin1

2. Reversible Changes in the State of Phosphorylation of Gizzard Myosin, in That of Gizzard Myosin Assembly, in the ATPase Activity of Gizzard Myosin, in That of Actomyosin and in the Superprecipitation Activity1

3. A bent monomeric conformation of myosin from smooth muscle.

4. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules

5. Correlation of enzymatic properties and conformation of smooth muscle myosin

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