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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1982-9-24
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pubmed:abstractText |
It is shown, by means of analytical ultracentrifugation, that skeletal myosin S-1 exists in the form of a monomer-dimer mixture, in rapid reversible equilibrium, sensitive to the hydrostatic pressure, the temperature, and the composition of the buffer (at least, pH, ionic strength, presence or absence of a Mg-(phosphate compound), and presence or absence of Mg2+). The dimer is predominant at high pH, at low ionic strength, in the presence of a Mg-(phosphate compound), at high pressure, and at low temperature. The monomer is predominant in the reverse conditions. At atmospheric pressure and at room temperature, in a buffer having a composition close to that of the physiological medium, but containing no Mg-(phosphate compound), the monomer is largely predominant (more than 90% at 1 mg/mL S-1). At atmospheric pressure and at room temperature, in a buffer containing a Mg-(phosphate compound) and having a composition close to that of the physiological medium, S-1 exists in the form of a monomer-dimer mixture, with a noticeable proportion of dimer (more than 25% at 1 mg/mL S-1 in the presence of 2 mM MgADP and 3 mM Mg2+). In such buffers, the monomer:dimer ratio is extremely sensitive to both the pH and the ionic strength. The sedimentation coefficients of the monomer and the dimer are respectively 5.05 +/- 0.05 S and 6.05 +/- 0.05 S. The two protomers making up the dimer are stuck together in an end-to-end arrangement. Both the monomer and the dimer are highly hydrated (about 0.9 g of water/g of protein for the monomer and probably more for the dimer).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Buffers,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2679-86
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7093215-Animals,
pubmed-meshheading:7093215-Buffers,
pubmed-meshheading:7093215-Chemistry, Physical,
pubmed-meshheading:7093215-Hydrogen-Ion Concentration,
pubmed-meshheading:7093215-Macromolecular Substances,
pubmed-meshheading:7093215-Magnesium,
pubmed-meshheading:7093215-Myosin Subfragments,
pubmed-meshheading:7093215-Myosins,
pubmed-meshheading:7093215-Osmolar Concentration,
pubmed-meshheading:7093215-Peptide Fragments,
pubmed-meshheading:7093215-Physicochemical Phenomena,
pubmed-meshheading:7093215-Rabbits,
pubmed-meshheading:7093215-Temperature,
pubmed-meshheading:7093215-Ultracentrifugation
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pubmed:year |
1982
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pubmed:articleTitle |
Dimerization of the myosin heads in solution.
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pubmed:publicationType |
Journal Article
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