Linked Life Data

2764944

Source:http://linkedlifedata.com/resource/pubmed/id/2764944

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-9-21
pubmed:abstractText
Glutathione S-transferase was found to be a good substrate of Ca++-phospholipid-dependent protein kinase in vitro. Of 6 isozymes of glutathione transferase purified from rat liver cytosol (1-1, 1-2, 2-2, 3-3, 3-4, 4-4), only isozymes 1-1, 1-2 and 2-2 were significantly phosphorylated by the kinase purified from rabbit brain. Phosphorylation was more pronounced in subunit 1 than in subunit 2, and the degree of the phosphorylation was similar in all three homo- and heterodimers, where 1 mol of phosphoryl group per mol subunit was transferred to the subunit 1. The phosphorylated transferase 1-1 showed decreased affinity for bilirubin, suggesting that the phosphorylation affects the function of glutathione S-transferase in an isozyme-specific manner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
903-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Glutathione S-transferase is an in vitro substrate of Ca++-phospholipid-dependent protein kinase (protein kinase C).
pubmed:affiliation
Institute of Experimental Pathology, German Cancer Research Center, Heidelberg.
pubmed:publicationType
Journal Article