Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion
Journal Article
·
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
- Univ. of Lund (Sweden)
Glutathione transferase mRNA levels were measured in human liver samples by using mouse and human cDNA clones that encode class-mu and class-alpha GT. Although all the RNA samples examined contained class-alpha GT mRNA, class-mu GT mRNA was found only in individuals whose peripheral leukocytes expressed GT activity on the substrate trans-stilbene oxide. The mouse class-mu cDNA clone was used to identify a human class-mu GT cDNA clone, {lambda}GTH411. The amino acid sequence of the GT encoded by {lambda}GTH411 is identical with the 23 residues determined for the human liver GT-{mu} isoenzyme and shares 76-81% identity with mouse and rat class-mu GT isoenzymes. The mouse and human class-mu GT cDNA inserts hybridize with multiple BamHI and EcoRI restriction fragments in the human genome. One of these hybridizing fragments is missing in the DNA of individuals who lack GT activity on trans-stilbene oxide. Hybridizations with nonoverlapping subfragments of {lambda}GTH411 suggest that there are at least three class-mu genes in the human genome. One of these genes appears to be deleted in individuals lacking GT activity on trans-stilbene oxide.
- OSTI ID:
- 5546979
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:19; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22
Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22
Cloning the mouse homologue of the human lysosomal acid {alpha}-glucosidase gene
Journal Article
·
Thu Jan 19 23:00:00 EST 1995
· Genomics
·
OSTI ID:250151
Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22
Journal Article
·
Sat Oct 01 00:00:00 EDT 1988
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
·
OSTI ID:5546873
Cloning the mouse homologue of the human lysosomal acid {alpha}-glucosidase gene
Journal Article
·
Thu Sep 01 00:00:00 EDT 1994
· American Journal of Human Genetics
·
OSTI ID:134629
Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY
BODY FLUIDS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
DNA
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
ENZYME ACTIVITY
ENZYMES
GENE MUTATIONS
GENE REGULATION
GENES
GLANDS
GLUTATHIONE
HYBRIDIZATION
ISOENZYMES
ISOTOPES
LEUKOCYTES
LIGHT NUCLEI
LIVER
MAMMALS
MAN
MATERIALS
MESSENGER-RNA
MOLECULAR STRUCTURE
MUTATIONS
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
POLYPEPTIDES
PRIMATES
PROTEINS
RADIOISOTOPES
RADIOPROTECTIVE SUBSTANCES
RECOMBINANT DNA
RNA
STRUCTURAL CHEMICAL ANALYSIS
TRANSFERASES
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY
BODY FLUIDS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
DNA
DNA SEQUENCING
DRUGS
ELECTROPHORESIS
ENZYME ACTIVITY
ENZYMES
GENE MUTATIONS
GENE REGULATION
GENES
GLANDS
GLUTATHIONE
HYBRIDIZATION
ISOENZYMES
ISOTOPES
LEUKOCYTES
LIGHT NUCLEI
LIVER
MAMMALS
MAN
MATERIALS
MESSENGER-RNA
MOLECULAR STRUCTURE
MUTATIONS
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
POLYPEPTIDES
PRIMATES
PROTEINS
RADIOISOTOPES
RADIOPROTECTIVE SUBSTANCES
RECOMBINANT DNA
RNA
STRUCTURAL CHEMICAL ANALYSIS
TRANSFERASES
VERTEBRATES