Linked Life Data

701276

Source:http://linkedlifedata.com/resource/pubmed/id/701276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1978-12-20
pubmed:abstractText
High mobility group proteins were isolated from calf thymus and duck erythrocyte nuclei and the possibility was investigated that these proteins undergo acetylation similar to that occurring in some histones. Dinitrophenylation of the proteins followed by acid hydrolysis and amino acid analysis indicated that 2 to 3% of the lysine residues present were unavailable for reaction with fluorodinitrobenzene. Extensive enzymatic degradation with trypsin and pronase and subsequent amino acid analysis showed a significant amount of material eluting at the position of epsilon-N-acetyllysine. Recovery and acid hydrolysis of this material generated a peak eluting in the lysine position. In vitro radioactive labeling of calf thymus nuclei with [3H]acetate yielded labeled high mobility group proteins. All of these findings are in accord with the conclusion that high mobility group proteins are acetylated and that acetylation occurs as a postsynthetic modification of these proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7601-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Postsynthetic modification of high mobility group proteins. Evidence that high mobility group proteins are acetylated.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.