Linked Life Data

6786353

Source:http://linkedlifedata.com/resource/pubmed/id/6786353

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-8-27
pubmed:abstractText
The epsilon-(gamma-glutamic)lysine cross-link content of glycerol-extracted cultured embryonic chick heart myofibrils is increased by treatment with Mg2+-ATP followed by Ca2+ but not by Ca2+ alone. Fractionation of protein chains dissolved in sodium dodecyl sulfate and dithiothreitol shows that the increase of cross-link content occurs in very large proteins (greater than 250 kdaltons) and that there is a very marked decrease in cross-link content in the 82 kdalton region. Treatment of the glycerol-extracted myofibrils with Mg2+-ATP followed by Ca2+ also increases the amount of protein in the very high molecular weight fraction and there is a corresponding reduction of material in some of the lighter chains particularly in fibronectin, actin and in 82 and 51 kdalton chains. The relevance of Mg2+-ATP plus Ca2+ -dependent Glu-Lys cross-link formation to cyclical or reversible cellular processes is discussed briefly.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
668
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Modulation of the epsilon-(gamma-glutamic)lysine cross-link in cellular proteins. II. Fractionation studies.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.