Linked Life Data

3401222

Source:http://linkedlifedata.com/resource/pubmed/id/3401222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-9-2
pubmed:abstractText
Fluorescent labeling, limited proteolysis, amino acid sequence determinations, affinity chromatography and specific chemical crosslinking were used to determine the smallest fragment of gizzard caldesmon that interacts with actin. The time course of cleavage with thrombin or submaxillaris arginase-C protease indicates that 90kDa and 35kDa fragments are the two major pieces of the 120kDa native protein. Amino acid sequence determination indicates that the 90kDa fragment is the N-terminal portion of the molecule. Further degradation gave rise to a 15kDa product whose N-terminal amino acid sequence was determined within the first 28 amino acids. Carbodiimide crosslinking with actin revealed that the 15kDa part of the molecule is probably not involved in the actin binding process but may participate in a twisting of the F-actin filament and be responsible of the caldesmon regulatory function during smooth muscle contraction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
564-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Identification of a 15 kilodalton actin binding region on gizzard caldesmon probed by chemical cross-linking.
pubmed:affiliation
Centre de Biochimie Macromoléculaire du CNRS, INSERM U 249, Université Montpelliér I, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't