Document Detail

Myosin phosphorylation in permeabilized rabbit psoas fibers.
MedLine Citation:
PMID:  4037077     Owner:  NLM     Status:  MEDLINE    
The 18,000-Da myosin light chains in segments of rabbit psoas fibers were stably phosphorylated to assess the mechanical effects of this modification. Before and after phosphorylation of the same fiber, the maximal shortening velocity (Vmax) was measured at 12 degrees C by a quick-release slack test and by extrapolation to Vmax of hyperbolic force-velocity curves from isotonic releases. The experiments were performed at saturating concentrations of Ca2+, as determined from isometric force-pCa curves, under conditions in which the pH and ATP-ADP ratio were buffered. No effect of phosphorylation on isometric force, Vmax, or the shape of the force-velocity curve was detected under conditions of maximal calcium activation. Thus we find no mechanical evidence for a modulation by light chain phosphorylation of actomyosin interaction in these fiber segments.
H L Sweeney; M J Kushmerick
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  249     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1985 Sep 
Date Detail:
Created Date:  1985-10-10     Completed Date:  1985-10-10     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  C362-5     Citation Subset:  IM    
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MeSH Terms
Calcium / pharmacology
Cell Membrane Permeability*
Electrophoresis, Polyacrylamide Gel
Isometric Contraction
Muscles / metabolism,  physiology*
Myosins / isolation & purification,  metabolism*
Grant Support
Reg. No./Substance:
7440-70-2/Calcium; EC

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