Linked Life Data

2869797

Source:http://linkedlifedata.com/resource/pubmed/id/2869797

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1986-5-7
pubmed:abstractText
The sensitivity of tissue transglutaminase to activation by Ca2+ and other cellular factors was investigated using the enzyme purified from rat liver. The inclusion of Mg2+ in the assay system appeared to reduce the Ca2+-requirement of the enzyme when native N,N'-dimethylcasein was used as the protein acceptor substrate. However, when this protein was dephosphorylated, the Ca2+-requirement was unaffected by Mg2+. In addition, using this modified assay, a Km for Ca2+ was calculated to be in the range of 3-4 microM, at least an order of magnitude lower than that obtained with native acceptor substrate. Membrane phospholipids, 1,2-diolein and calmodulin were found not to affect the activation of transglutaminase by Ca2+. The sensitivity of transglutaminase to Ca2+ which we have now demonstrated suggests that this enzyme may directly act as a receptor protein for Ca2+ during stimulus-response coupling mediated by this cation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0144-8463
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1079-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't