Linked Life Data

2879405

Source:http://linkedlifedata.com/resource/pubmed/id/2879405

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-2-6
pubmed:abstractText
Interrelation between the effects of C-protein and LC2-light chains on actin-activated ATPase activity of skeletal muscle myosin has been investigated at various ionic strength (0.06-0.14) and free calcium levels (10(-4) M, 10(-8) M). The ATPase activity of AM reconstituted with column-purified myosin or partly-purified myosin and non-regulated actin exhibits a pronounced dependence on ionic strength with maximum at I = 0.1. C-protein impurities (5 per cent) usually present in Minit can inhibit AM ATPase at every ionic strength assayed, without changing the character of this dependence. Actin-activated ATPase of the above myosins shows calcium sensitivity at every ionic strength studied. The partial removal of LC2 from Mcol results in a decrease of AM ATPase and in a disappearance of its calcium sensitivity. C-protein added to Mcol in a molar ratio of 1:1 inhibits considerably AM ATPase, reduces its sensitivity to ionic strength and abolishes its calcium sensitivity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0237-6261
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-56
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Effect of C-protein and LC-light chains on actomyosin ATPase at various ionic strength and calcium levels.
pubmed:publicationType
Journal Article, In Vitro