Linked Life Data

9925755

Source:http://linkedlifedata.com/resource/pubmed/id/9925755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-3-15
pubmed:abstractText
Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. Purification of PARG from many tissues revealed heterogeneity in activity and structure of this enzyme. To investigate PARG structure and localization, we developed a highly sensitive one-dimensional zymogram allowing us to analyze PARG activity in crude extracts of Cos-7, Jurkat, HL-60, and Molt-3 cells. In all extracts, a single PARG activity band corresponding to a protein of about 110 kDa was detected. This 110-kDa PARG activity was found mainly in cytoplasmic rather than in nuclear extracts of Cos-7 cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
246
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
395-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein.
pubmed:affiliation
CHUL Research Center, CHUQ, Laval University, Sainte-Foy, Québec, G1V 4G2, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't