Linked Life Data

7664797

Source:http://linkedlifedata.com/resource/pubmed/id/7664797

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1995-10-10
pubmed:abstractText
The finding that recently cloned mono-ADP-ribosyltransferases show sequence similarity to the rat T cell differentiation marker RT6 has led us to investigate the enzymatic activity of this alloantigenic system. To search for ADP-ribosylation of cell surface proteins, T cell populations from RT6.1- and RT6.2-expressing rat strains, as well as RT6.1+ and RT6.2+ T-T hybridoma cell lines, were incubated with [32P]nicotinamide adenine dinucleotide (NAD). All RT6.2+, but no RT6.1+ or RT6- cells, show incorporation of radioactivity into a single protein which could be identified as RT6.2 by immunoprecipitation with monoclonal antibodies. This automodification of RT6.2 is covalent, requires intact NAD as substrate, and displays characteristics typical for linkage of ADP-ribose to arginine. The alloantigens RT6.1 and RT6.2 differ in ten amino acids, RT6.2 having two arginine residues not present in RT6.1. Both alloantigens were found to display potent NAD-glycohydrolase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2355-61
pubmed:dateRevised
2009-9-7
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Both allelic forms of the rat T cell differentiation marker RT6 display nicotinamide adenine dinucleotide (NAD)-glycohydrolase activity, yet only RT6.2 is capable of automodification upon incubation with NAD.
pubmed:affiliation
Department of Immunology, Eppendorf University Hospital, Hamburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't