Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases.
Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was determined and showed a typical class Alpha GSH transferase structure including an N-acetylated N-terminal methionine residue.
Alin
P
P
Department of Biochemistry, University of Stockholm, Sweden.
Jensson
H
H
Cederlund
E
E
Jörnvall
H
H
Mannervik
B
B
D000595:Amino Acid Sequence; D000818:Animals; D003600:Cytosol / Q000201:enzymology*; D005982:Glutathione Transferase / Q000145:classification* / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D005982:Glutathione Transferase