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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1989-10-18
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pubmed:abstractText |
Tumor cells resistant to chloroethylnitrosourea (CENU) therapy contain high levels of O6-alkylguanine DNA-alkyltransferase (GATase), a DNA repair enzyme that aborts DNA interstrand cross-linking by removing CENU-induced O6-alkylguanine adducts. Because the transferase binds covalently to CENU-treated oligonucleotides, we reacted partially purified GATase from cultured human lymphoblasts with a BCNU-treated, 35S-5'-end-labeled, synthetic oligonucleotide designed to have a polyadenylated 3' terminus. Immunoprobing Western blots of this reaction mixture with GATase-specific monoclonal antibody indicated that 25-30% of the transferase became complexed. We purified this complex by affinity chromatography with oligo(dT) cellulose, recovering homogenous material that appeared as a discrete 35-kDa Coomassie blue or silver-stained band after SDS-polyacrylamide gel electrophoresis. Autoradiography and Western immunoblotting confirmed that this band contained both the radiolabeled oligonucleotide and the GATase protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3004713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3079405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3355582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3405749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3679391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3708569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3731392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3814140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3857628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3916338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-3960738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6325181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6585269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6822564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6870930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6947250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-6957878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-7279663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-7380020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2780288-7464910
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6581-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2780288-Base Sequence,
pubmed-meshheading:2780288-Blotting, Western,
pubmed-meshheading:2780288-Carmustine,
pubmed-meshheading:2780288-Cell Line,
pubmed-meshheading:2780288-Chromatography, Affinity,
pubmed-meshheading:2780288-Humans,
pubmed-meshheading:2780288-Kinetics,
pubmed-meshheading:2780288-Methyltransferases,
pubmed-meshheading:2780288-Molecular Sequence Data,
pubmed-meshheading:2780288-Molecular Weight,
pubmed-meshheading:2780288-O(6)-Methylguanine-DNA Methyltransferase,
pubmed-meshheading:2780288-Oligodeoxyribonucleotides,
pubmed-meshheading:2780288-Protein Binding
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pubmed:year |
1989
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pubmed:articleTitle |
Affinity purification and characterization of human O6-alkylguanine-DNA alkyltransferase complexed with BCNU-treated, synthetic oligonucleotide.
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pubmed:affiliation |
Department of Biochemical and Clinical Pharmacology, St. Jude Children's Research Hospital, Memphis, TN 38101.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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