Linked Life Data

8376398

Source:http://linkedlifedata.com/resource/pubmed/id/8376398

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1993-10-20
pubmed:abstractText
The functional significance of the large number of myosin isoforms in skeletal muscles is poorly understood. Myosin molecules that have the same heavy chain, but differ in their essential or alkali light chains, have the same actin-activated ATPase activity. Similarly, the many heavy chain isoforms that appear during the course of muscle development do not show any significant differences in enzymatic activity. By means of an in vitro motility assay, we have measured the analogue of unloaded shortening velocity for myosin isoforms in a reconstituted actomyosin system. We find that both light and heavy chain isoforms translocate actin filaments at distinct velocities. These results support the hypothesis that myosin isoforms are the primary determinant for the range of shortening velocities adopted by a muscle in response to changing functional demands.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20414-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay.
pubmed:affiliation
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't