Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12
The glutathione S-transferases (GST) (glutathione transferase; EC 2.5.1.18) are a family of enzymes responsible for the metabolism of a broad range of xenobiotics and carcinogens. A cDNA clone containing the entire amino acid coding sequence of a human GST-2 subunit has been isolated using a lambdagt11 expression library. The complete nucleotide sequence and a partial restriction map are presented. The subunit is composed of 221 amino acids with a molecular weight of 25,425 before post translational modification. The deduced amino acid sequence is rich in lysine, which is consistent with the relatively high pI of GST-2. The human sequence shows considerable homology with the rat Ya and Yc GST sequences but little homology with the rat GSTp and Yb subunit sequences. Southern blots of restriction digests of human DNA indicate that there may be multiple GST-2 genes. In situ hybridization of the cloned cDNA to human chromosomes produces intense labeling only over band p12 on the short arm of chromosome 6 near the centromere. This indicates that the GST-2 gene(s) are located only at this site.
- Research Organization:
- Australian National Univ., Canberra
- OSTI ID:
- 6027033
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 84:8; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CARBOXYLIC ACIDS
CARCINOGENS
CHROMOSOMES
DAYS LIVING RADIOISOTOPES
DNA
DNA SEQUENCING
ELECTROPHORESIS
ENZYMES
GENETIC MAPPING
HYBRIDIZATION
ISOTOPES
LABELLED COMPOUNDS
LIGHT NUCLEI
LYSINE
MAMMALS
MAPPING
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
RADIOISOTOPES
RATS
RECOMBINANT DNA
RODENTS
STRUCTURAL CHEMICAL ANALYSIS
TRANSFERASES
TRITIUM COMPOUNDS
VERTEBRATES
XENOBIOTICS