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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1998-7-2
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pubmed:databankReference | |
pubmed:abstractText |
Two novel major heterodimeric Mu-class glutathione (GSH) S-transferases (GSTs), designated M1-2 and M1-3*, were isolated from guinea pig (gp) liver cytosol and purified to homogeneity together with a known major homodimeric Mu-class gpGSTM1-1 (reported as GST b by R. Oshino, K. Kamei, M. Nishioka, and M. Shin, 1990, J. Biochem. 107, 105-110). These three gpGSTs were quantitatively retained on an S-hexyl-GSH affinity column and separated as homogeneous proteins by chromatofocusing. Subunits of the heterodimers were inseparable on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, but could be completely separated by reverse-phase partition high-performance liquid chromatography. A molecular cloning study demonstrated that the gpGST subunit M2 consisted of 217 amino acid residues with a calculated molecular mass of 25,562 and shared 84% identity in overall amino acid sequence with gpGSTM1-1. N-terminal amino acid sequences of peptides from the gpGST subunit M3* with a blocked N-terminus strongly suggested that it should belong to the Mu class. Western blot analysis using antisera raised against purified rat (r) GSTsA1-2 (Alpha), M1-1, P1-1 (Pi), and T2-2 (Theta) indicated that gpGSTsM1-1 and M1-3* cross-reacted only with anti-rGSTM1 antibody. However, gpGSTM1-2 cross-reacted intensely to almost the same extent with antibodies to both rGSTsM1-1 and T2-2. A homodimeric gpGSTM2-2, artificially constructed from native gpGSTM1-2 by treatment with guanidine hydrochloride followed by dialysis, intensely cross-reacted with antibodies to both the rat Mu- and Theta-class GSTs. Thus, the gpGST subunit M2 provided the first evidence for the double immuno-cross-reaction of a GST with polyclonal antibodies to two different classes of GSTs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
354
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
188-96
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:9633615-Amino Acid Sequence,
pubmed-meshheading:9633615-Animals,
pubmed-meshheading:9633615-Antibodies,
pubmed-meshheading:9633615-Cloning, Molecular,
pubmed-meshheading:9633615-Cross Reactions,
pubmed-meshheading:9633615-Cytosol,
pubmed-meshheading:9633615-DNA, Complementary,
pubmed-meshheading:9633615-Dimerization,
pubmed-meshheading:9633615-Glutathione Transferase,
pubmed-meshheading:9633615-Guinea Pigs,
pubmed-meshheading:9633615-Liver,
pubmed-meshheading:9633615-Male,
pubmed-meshheading:9633615-Molecular Sequence Data,
pubmed-meshheading:9633615-Rats
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pubmed:year |
1998
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pubmed:articleTitle |
Guinea pig liver Mu-class glutathione S-transferase M1-2 cross-reacts with antibodies to both rat Mu- and theta-class glutathione S-transferases.
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pubmed:affiliation |
Department of Drug Metabolism and Molecular Toxicology, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Japan.
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pubmed:publicationType |
Journal Article
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