scholarly journals Rat liver glutathione S-transferases. Complete nucleotide sequence of a glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital.

1984 ◽  
Vol 259 (8) ◽  
pp. 5182-5188 ◽  
Author(s):  
C B Pickett ◽  
C A Telakowski-Hopkins ◽  
G J Ding ◽  
L Argenbright ◽  
A Y Lu
Keyword(s):  
Nucleotide Sequence ◽  
Rat Liver ◽  
Complete Nucleotide Sequence ◽  
Glutathione S Transferase ◽  
Liver Glutathione ◽  
Glutathione S Transferases

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 Rat lung glutathione S-transferases. Evidence for two distinct types of 22000-Mr subunits

1984 ◽  
Vol 221 (3) ◽  
pp. 609-615 ◽  
Author(s):  
S V Singh ◽  
C A Partridge ◽  
Y C Awasthi
Keyword(s):  
Rat Liver ◽  
The Other ◽  
Rat Lung ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
Liver Glutathione ◽  
Immunological Properties ◽  
Glutathione S Transferases

Two immunologically distinct types of 22000-Mr subunits are present in rat lung glutathione S-transferases. One of these subunits is probably similar to Ya subunits of rat liver glutathione S-transferases, whereas the other subunit Ya′ is immunologically distinct. Glutathione S-transferase II (pI7.2) of rat lung is a heterodimer (YaYa′) of these subunits, and glutathione S-transferase VI (pI4.8) of rat lung is a homodimer of Ya′ subunits. On hybridization in vitro of the subunits of glutathione S-transferase II of rat lung three active dimers having pI values 9.4, 7.2 and 4.8 are obtained. Immunological properties and substrate specificities indicate that the hybridized enzymes having pI7.2 and 4.8 correspond to glutathione S-transferases II and VI of rat lung respectively.

scholarly journals Studies on the subunit composition of rat liver glutathione S-transferases.

1983 ◽  
Vol 258 (18) ◽  
pp. 11321-11325 ◽  
Author(s):  
A B Frey ◽  
T Friedberg ◽  
F Oesch ◽  
G Kreibich
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

Subunit composition of rat liver glutathione S-transferases

1982 ◽  
Vol 108 (2) ◽  
pp. 461-467 ◽  
Author(s):  
Chen-Pei D. Tu ◽  
Mitchell J. Weiss ◽  
C. Channa Reddy
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

scholarly journals Inhibition by inorganic anions of glutathione S-transferases from insect and mammalian sources

1991 ◽  
Vol 278 (1) ◽  
pp. 193-198 ◽  
Author(s):  
A G Clark ◽  
J F Hamilton ◽  
S N Marshall
Keyword(s):  
Rat Liver ◽  
Galleria Mellonella ◽  
Limited Range ◽  
Inorganic Anions ◽  
Glutathione S Transferase ◽  
Inhibitory Potency ◽  
Glutathione S Transferases ◽  
Wax Moth

Glutathione S-transferases 1-1, 3-3, 3-4 and 4-4 from rat liver and the major glutathione S-transferase from the wax moth (Galleria mellonella) are all inhibited by several simple inorganic anions. For each of 3-3, 3-4 and the insect enzyme, the order of inhibitory potency was ClO4- greater than or equal to SCN- greater than I- greater than NO3- greater than Br-. A more limited range of anions was tested on the isoenzymes 1-1 and 4-4, but the same trend was apparent. Values for Ki ranged from about 200 mM for Cl- to 6 mM for SCN- in the case of the insect enzyme and from 50 mM for Br- to 0.3 mM for SCN- for the rat isoform 3-3. Acetate, F-, SO4(2-) and PO4(3-) were not found to have significant inhibitory properties. The mode of inhibition was characterized as non-competitive in the case of the insect enzyme and rat transferase 1-1, whereas the mode of inhibition was partially non-competitive in the case of the rat isoforms 3-3, 3-4 and 4-4.

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