Linked Life Data

2167519

Source:http://linkedlifedata.com/resource/pubmed/id/2167519

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-9-27
pubmed:abstractText
Isolated rat enterocytes were incubated with E. coli heat-stable enterotoxin or buffer alone and the protein kinase activity and cyclic GMP level determined on the particulate fraction or cytosol, respectively. In the control cells, particulate protein kinase activity and cyclic GMP concentration were at a maximum after 20 sec and 1 min of incubation, respectively. In heat-stable enterotoxin-treated cells the particulate protein kinase activity was significantly increased (P less than 0.05) after 20 sec of incubation, but decreased (P less than 0.05) after 30 sec, 1 min and 2 min, when compared to the control reaction. During this time period the concentration of intracellular cyclic GMP increased 10-fold. The effect of heat-stable enterotoxin on particulate protein kinase activity and cyclic GMP concentration was dose-dependent. Analysis of radioactive membrane phosphorylation products indicate a role for phosphoproteins with a mol. wt of 25,000 and 120,000. These results suggest that the action of heat-stable enterotoxin may involve an effect on protein kinase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
493-500
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The effect of Escherichia coli heat-stable enterotoxin on protein kinase activity.
pubmed:affiliation
Department of Medical Microbiology, Creighton University School of Medicine, Omaha, NE.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.