Linked Life Data

465557

Source:http://linkedlifedata.com/resource/pubmed/id/465557

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1979-10-24
pubmed:abstractText
The phalloidin addition (20--30 mkg/ml) is shown to be followed by complex transient of isometric tension of fibres in low Ca++ concentration. The process is accelerated by the temperature increase. The phalloidin treatment does not cause the loss of contractility and Ca++-sensitivity of isometric tension. The treated fibres lost their ability to work in an autooscillation mode at 20--23 degrees C but were in condition to do this at the temperatures higher than 30 degrees C. The mechanical properties of rigor fibres as well at the myosin aggregation dependence on ionic strength were not markedly changed after the treatment. The results make it possible to conclude that the autooscillation mode of contraction is due to some feedback via I-filaments. The actin modification by phalloidin disturbs this feedback.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3029
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
509-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Effect of phalloidine on the contractile properties of glycerinized skeletal muscle].
pubmed:publicationType
Journal Article, English Abstract