Linked Life Data

3042023

Source:http://linkedlifedata.com/resource/pubmed/id/3042023

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1988-9-9
pubmed:abstractText
Troponin I (TnI) is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium sensitivity to striated muscle actomyosin ATPase activity. We have determined the amino acid sequence of TnI from adult bovine cardiac muscle. This protein is a single polypeptide chain of 211 amino acids with an acetylated amino terminus, a calculated molecular weight of 23,975, and a net charge of +17 at neutral pH. There was no evidence for heterogeneity of the sequence. Comparison with other available TnI sequences shows an amino-terminal extension of 27-33 residues which is present in cardiac but not skeletal TnI. The remainder of the polypeptide is common to both cardiac and skeletal TnI. In the amino-terminal half of the common polypeptide, only 29% of the residues are invariant in all sequences. The carboxyl-terminal half (residues 124-210) is much more highly conserved, with 66% invariant residues. Bovine cardiac TnI and rabbit cardiac TnI are very similar in sequence: only 12 of 26 residues are identical in the amino-terminal segments, but the remaining residues of the proteins are 97% identical.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2821-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Amino acid sequence of bovine cardiac troponin I.
pubmed:affiliation
Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.