Publication Date:
1979-05-04
Description:
Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca2+-and Sr2+-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca2+- and Sr2+-activated tensions. Adenosine 5'-O (3'-thiotriphosphate) only in the presence of Ca2+ induced irreversible Ca2+-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of 32P from [gamma-32P]adenosine triphosphate into the myosin light chains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoar, P E -- Kerrick, W G -- Cassidy, P S -- New York, N.Y. -- Science. 1979 May 4;204(4392):503-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432654" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Calcium/*pharmacology
;
Chickens
;
Gizzard/*physiology
;
In Vitro Techniques
;
Molecular Weight
;
Muscle Contraction/*drug effects
;
Muscle, Smooth/*physiology
;
Myosins/*metabolism
;
Phosphorylation
;
Protein Kinases/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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