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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
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pubmed:dateCreated |
1985-11-29
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pubmed:abstractText |
The influence of Ca2+ on the enzymatic and physical properties of smooth muscle myosin was studied. The actin-activated ATPase activity of phosphorylated gizzard myosin and heavy meromyosin is higher in the presence of Ca2+ than in its absence, but this effect is found only at lower MgCl2 concentrations. As the MgCl2 concentration is increased, Ca2+ sensitivity is decreased. The concentration of Ca2+ necessary to activate ATPase activity is higher than that required to saturate calmodulin. The similarity of the pCa dependence of ATPase activity and of Ca2+ binding to myosin and the competition by Mg2+ indicate that these effects involved the Ca2+-Mg2+ binding sites of gizzard myosin. For the actin dependence of ATPase activity of phosphorylated myosin at low concentrations of MgCl2, both Vmax and Ka are influenced by Ca2+. The formation of small polymers by phosphorylated myosin in the presence of Ca2+ could account for the alteration in the affinity for actin. For the actin dependence of phosphorylated heavy meromyosin at low MgCl2 concentrations, Ca2+ induces only an increase in Vmax. To detect alterations in physical properties, two techniques were used: viscosity and limited papain hydrolysis. For dephosphorylated myosin, 6 S or 10 S, Ca2+-dependent effects are not detected using either technique. However, for phosphorylated myosin the decrease in viscosity corresponding to the 6 S to 10 S transition is shifted to lower KCl concentrations by the presence of Ca2+. In addition, a Ca2+ dependence of proteolysis rates is observed with phosphorylated myosin but only at low ionic strength, i.e. under conditions where myosin assumes the folded conformation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Papain,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13146-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2932435-Actins,
pubmed-meshheading:2932435-Adenosine Triphosphatases,
pubmed-meshheading:2932435-Animals,
pubmed-meshheading:2932435-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:2932435-Calcium,
pubmed-meshheading:2932435-Enzyme Activation,
pubmed-meshheading:2932435-Gizzard,
pubmed-meshheading:2932435-Magnesium,
pubmed-meshheading:2932435-Magnesium Chloride,
pubmed-meshheading:2932435-Muscle, Smooth,
pubmed-meshheading:2932435-Myosin Subfragments,
pubmed-meshheading:2932435-Myosins,
pubmed-meshheading:2932435-Papain,
pubmed-meshheading:2932435-Phosphorylation,
pubmed-meshheading:2932435-Protein Conformation,
pubmed-meshheading:2932435-Tropomyosin,
pubmed-meshheading:2932435-Turkeys
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pubmed:year |
1985
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pubmed:articleTitle |
Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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