Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver.
More than 85% of the complete amino-acid sequence of the alpha-class glutathione S-transferase omega (GST omega) of human liver, described for the first time in this communication, show that GST omega is a heterodimer of two closely related novel alpha-class GST subunits. The sequences of these subunits, omega 1 and omega 2, have over 97% homology between them and are also highly homologous to the two alpha-class subunits characterized previously. Characterization of these two novel alpha-class subunits described in this report would explain the molecular basis for high degree of heterogeneity observed among the alpha-class human GSTs.
Ahmad
H
H
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston 77555-1067.
Singhal
S S
SS
Saxena
M
M
Awasthi
Y C
YC
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D005982:Glutathione Transferase