Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA

1987 ◽  
Vol 15 (4) ◽  
pp. 734-736 ◽  
Author(s):  
CHEN-PEI D. TU ◽  
BIAO QIAN
Keyword(s):  
Nucleotide Sequence ◽  
Human Liver ◽  
Glutathione S Transferase ◽  
Liver Glutathione

scholarly journals The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone.

1984 ◽  
Vol 259 (9) ◽  
pp. 5536-5542
Author(s):  
H C Lai ◽  
N Li ◽  
M J Weiss ◽  
C C Reddy ◽  
C P Tu
Keyword(s):  
Nucleotide Sequence ◽  
Rat Liver ◽  
Cdna Clone ◽  
Glutathione S Transferase ◽  
Liver Glutathione

scholarly journals Human liver glutathione S-transferase ψ. Chemical characterization and secondary-structure comparison with other mammalian glutathione S-transferases

1987 ◽  
Vol 243 (1) ◽  
pp. 61-67 ◽  
Author(s):  
S V Singh ◽  
A Kurosky ◽  
Y C Awasthi
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Human Liver ◽  
Chemical Characterization ◽  
Compositional Analysis ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Glutathione S Transferase ◽  
Structure Comparison ◽  
Liver Glutathione

The isolation and chemical characterization of the anionic human liver glutathione S-transferase (GST) psi (pI 5.5) are described and compared with other GST isoenzymes reported for rat and human. Amino acid compositional analysis, substrate specificity and isoelectric focusing indicated that GST psi is a unique isoenzyme form of GST. Strikingly, however, amino acid sequence analysis of the N-terminal region indicated that GST psi was identical with GST mu in the first 23 amino acid residues reported. It is likely that these two enzyme forms are at least partially structurally related. In order to investigate further the genetic relationship of GST psi to other reported GST isoenzymes, secondary-structure analysis was performed. Despite substantial differences in the N-terminal-region amino acid sequences of some of the GST isoenzymes, the secondary structure of all the isoenzymes is highly conserved at their N-termini. The general uniformity of the secondary structure of this enzyme class at their N-termini strongly indicated that the observed diversity of these isoenzymes probably occurred as a result of a mechanism of gene duplication followed by divergence rather than a mechanism of convergent evolution.

scholarly journals NewSacl RFLP for human liver glutathione-S-transferase

1991 ◽  
Vol 19 (1) ◽  
pp. 199-199
Author(s):  
D.C.Van Dyke ◽  
J. Roby ◽  
C.-P.D. Tu
Keyword(s):  
Human Liver ◽  
Glutathione S Transferase ◽  
Liver Glutathione

scholarly journals Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase δ is composed of two distinct subunits (B1 and B2)

1985 ◽  
Vol 227 (2) ◽  
pp. 457-465 ◽  
Author(s):  
P K Stockman ◽  
G J Beckett ◽  
J D Hayes
Keyword(s):  
Isoelectric Point ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Human Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Glutathione S Transferase ◽  
Liver Glutathione ◽  
Glutathione S Transferases

The purification of a hybrid glutathione S-transferase (B1 B2) from human liver is described. This enzyme has an isoelectric point of 8.75 and the B1 and B2 subunits are distinguishable immunologically and are ionically distinct. Hybridization experiments demonstrated that B1 B1 and B2 B2 could be resolved by CM-cellulose chromatography and have pI values of 8.9 and 8.4 respectively. Transferase B1 B2, and the two homodimers from which it is formed, are electrophoretically and immunochemically distinct from the neutral enzyme (transferase mu) and two acidic enzymes (transferases rho and lambda). Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis demonstrated that B1 and B2 both have an Mr of 26 000, whereas, in contrast, transferase mu comprises subunits of Mr 27 000 and transferases rho and lambda both comprise subunits of Mr 24 500. Antisera raised against B1 or B2 monomers did not cross-react with the neutral or acidic glutathione S-transferases. The identity of transferase B1 B2 with glutathione S-transferase delta prepared by the method of Kamisaka, Habig, Ketley, Arias & Jakoby [(1975) Eur. J. Biochem. 60, 153-161] has been demonstrated, as well as its relationship to other previously described transferases.

scholarly journals The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hbsubunit cDNA

1988 ◽  
Vol 16 (17) ◽  
pp. 8541-8554 ◽  
Author(s):  
Jeff L. DeJong ◽  
Chi-Ming Chang ◽  
Jacqueline Whang-Peng ◽  
Turid Knutsen ◽  
Chen-Pei D. Tu
Keyword(s):  
Human Liver ◽  
Chromosome Mapping ◽  
Glutathione S Transferase ◽  
Liver Glutathione ◽  
Transferase Gene
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