Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-2-24
pubmed:abstractText
It was found that extracts from human brain catalyzed the transfer of methyl groups from O6-methylguanine in methylated double-stranded DNA to a cysteine residue in a protein of mol. wt. approximately 22 000. This O6-alkylguanine-DNA alkyltransferase had properties similar to those previously characterized from rodent liver, human liver, cultured human cells and E. coli. The alkyltransferase activity of human brain was considerably greater than that reported for rat brain, but was significantly less than the activities found in human liver and other tissues. The activity was found in both normal brain samples (peritumoral material which contained no tumor infiltration) and in a variety of brain tumors. The highest activity was found in meningeomas and neurinomas, but most tumors with the exception of some gliomas had higher activities than the normal brain. All 23 tumor samples examined in this study had alkyltransferase activity in contrast to published reports showing that approximately 35% of human brain-tumor-derived lines grown in culture lacked this activity. This discrepancy may be due to the cellular polymorphism of the tumors, but also suggests that complete lack of the alkyltransferase is not a common occurrence in human brain tumors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0143-3334
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
O6-alkylguanine-DNA alkyltransferase activity in human brain and brain tumors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.