Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1982-7-8
|
pubmed:abstractText |
Myosin and F-actin were prepared from bovine carotid arterial smooth muscle and the properties of the binding of myosin to F-actin were compared with those of the binding of skeletal muscle myosin to F-actin. The following differences were observed between skeletal and smooth muscle myosins. 1. The rate of ATP-induced dissociation of arterial actomyosin was equal to that of hybrid actomyosin reconstituted from arterial myosin and skeletal muscle F-actin, but was much lower than those of skeletal muscle actomyosin and of hybrid actomyosin reconstituted from skeletal muscle myosin and arterial F-actin. 2. The amount of ATP necessary for complete dissociation of arterial actomyosin was 2 mol/mol of myosin, although it is well known that skeletal muscle actomyosin is dissociated completely by the addition of 1 mol ATP per mol of myosin. 3. Arterial actomyosin and hybrid actomyosin reconstituted from arterial myosin and skeletal muscle F-actin did not dissociate upon addition of 0.1 mM PPi, while skeletal muscle actomyosin dissociated completely. 4. In the absence of Mg2+, neither dissociation by ATP nor ATPase [EC 3.6.1.3] activity was observed with arterial actomyosin and hybrid actomyosin reconstituted from arterial myosin and skeletal muscle F-actin. On the other hand, skeletal muscle actomyosin dissociated almost completely upon addition of ATP and showed a considerably high ATPase activity. These observations reveal marked differences between myosins from skeletal and smooth muscles in their binding properties to F-actin.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Actomyosin,
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/EDTA-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0021-924X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
91
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1001-7
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:6122681-Actins,
pubmed-meshheading:6122681-Actomyosin,
pubmed-meshheading:6122681-Adenosine Triphosphatases,
pubmed-meshheading:6122681-Animals,
pubmed-meshheading:6122681-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:6122681-Carotid Arteries,
pubmed-meshheading:6122681-Cattle,
pubmed-meshheading:6122681-Kinetics,
pubmed-meshheading:6122681-Magnesium,
pubmed-meshheading:6122681-Muscle, Smooth,
pubmed-meshheading:6122681-Muscles,
pubmed-meshheading:6122681-Myosins,
pubmed-meshheading:6122681-Rabbits
|
pubmed:year |
1982
|
pubmed:articleTitle |
Differences between smooth and skeletal muscle myosins in their interactions with F-actin.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|