Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-3-20
pubmed:databankReference
pubmed:abstractText
The further biochemical characterization and subcellular localization of cardiotin, a high molecular weight (300 kDa) constituent of cardiac muscle, is described. Immunofluorescence assays revealed a colocalization of cardiotin and the Ca2+ pump SERCA2a in the longitudinal sarcoplasmic reticulum (SR). However, in contrast to SERCA2a, cardiotin is not detected in the junctional SR. Differential centrifugation experiments show that cardiotin cosediments with the microsomal fraction of swine heart, while differential extraction demonstrates that cardiotin is associated with the SR membranes. In the SR enriched cell fraction a 60 and a 100 kDa protein band are detected. Microsequence analyses of these two fragments showed a common amino-terminus of 14 amino acids, with great homology to amino acid positions 11-24 of human skeletal muscle alpha-actinin. Second generation antibodies directed to these specific fragments show the typical cardiotin pattern in cardiomyocytes and cross-reactivity amongst the respective antigens. Cardiotin did not colocalize with alpha-actinin, and alpha-actinin could not be detected in the microsomal SR fraction. Cardiotin therefore represents a new SR associated constituent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
403
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
168-72
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Biochemical characterization of cardiotin, a sarcoplasmic reticulum associated protein.
pubmed:affiliation
Department of Molecular Cell Biology and Genetics, University of Maastricht, The Netherlands. gert.schaart@molcelb.unimaas.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't