Linked Life Data

15795915

Source:http://linkedlifedata.com/resource/pubmed/id/15795915

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-4-4
pubmed:abstractText
Erythrocyte alpha-spectrin is ubiquitinated in repeats alpha20/alpha21, which also represents the nucleation site for contact with the beta subunit which leads to heterodimer formation by a zippering mechanism. In this study we have determined the second-order rate constant for association of ubiquitinated alpha'-spectrin, nonubiquitinated alpha-spectrin, and beta-spectrin into the alpha'beta or alphabeta heterodimer. The rate constant for incorporation of monomers into heterodimers at 37 degrees C were (5.181 +/- 0.001) x 10(5) M(-1) sec(-1) for total alpha-spectrin (alpha + alpha'), (5.121 +/- 0.001) x 10(5) M(-1) sec(-1) for alpha'-spectrin, and (5.178 +/- 0.003) x 10(5) M(-1) sec(-1) for beta-spectrin. We conclude that ubiquitination of alpha-spectrin does not regulate heterodimer formation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0361-8609
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Ubiquitination of red blood cell alpha-spectrin does not affect heterodimer formation.
pubmed:affiliation
Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, Texas 75083-0688, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.