Publication Date:
1985-06-14
Description:
Rapid laser pulse-induced photolysis of an adenosine triphosphate precursor in muscle fibers abruptly initiated cycling of the cross-bridges. The accompanying changes in tension and stiffness were related to elementary mechanochemical events of the energy-transducing mechanism. When inorganic phosphate was present at millimolar concentrations during liberation of adenosine triphosphate in the absence of calcium, relaxation was accelerated. Steady active tension in the presence of calcium was decreased but the approach to final tension was more rapid. These results suggest that, during energy transduction, formation of the dominant force-generating cross-bridge state is coupled to release of inorganic phosphate in a reaction that is readily reversible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hibberd, M G -- Dantzig, J A -- Trentham, D R -- Goldman, Y E -- AM00745/AM/NIADDK NIH HHS/ -- HL15835/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1317-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3159090" target="_blank"〉PubMed〈/a〉
Keywords:
Actomyosin/*metabolism
;
Adenosine Triphosphatases/metabolism
;
Adenosine Triphosphate/metabolism
;
Animals
;
Calcium/physiology
;
In Vitro Techniques
;
*Muscle Contraction
;
Muscles/*physiology
;
Phosphates/*metabolism
;
Rabbits
;
Viscosity
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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