Document Detail

Some effects of pressure treatment on actomyosin systems.
MedLine Citation:
PMID:  136239     Owner:  NLM     Status:  MEDLINE    
Natural actomyosin, actin and myosin, have been pressurized at up to 150 MN/m2 for 1 h at 0 degrees C and examined 3-5 h later. Pressurization of myosin resulted in the formation of aggregates with a molecular weight approximately that expected for a dimer, whereas with F-actin depolymerization occurred. With actomyosin, a gel to sol transition was promoted. Viscosity and light-scattering measurements indicated that pressurization results in a large measure of disaggregation of actomyosin in solution. Pressurization of actomyosin resulted in a greater decrease in the calcium-sensitive, than in the calcium-independent, Mg2+ ATPase activity. The Ca2+ and K+-EDTA ATPase activities of myosin were inhibited to about the same extent.
J M O'Shea; D J Horgan; J J Macfarlane
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Australian journal of biological sciences     Volume:  29     ISSN:  0004-9417     ISO Abbreviation:  Aust. J. Biol. Sci.     Publication Date:  1976 Jul 
Date Detail:
Created Date:  1976-12-23     Completed Date:  1976-12-23     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370613     Medline TA:  Aust J Biol Sci     Country:  AUSTRALIA    
Other Details:
Languages:  eng     Pagination:  197-207     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphatases / analysis
Hydrostatic Pressure*
Molecular Weight
Scattering, Radiation
Reg. No./Substance:
0/Actins; 0/Colloids; 0/Gels; 9013-26-7/Actomyosin; EC 3.6.1.-/Adenosine Triphosphatases; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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