Purification and characterization of glutathione S-transferase isozymes in dog lens.
1. Two isozymes of glutathione S-transferase (GST-dl1 and GST-dl2) were purified to homogeneity from dog lens. 2. The subunit size and the isoelectric point were determined to be 24,000 and > pI 9.5 for GST-dl1 and 22,000 and pI 8.1 for GST-dl2. 3. It was judged that GST-dl1 is a class alpha enzyme and GST-dl2 belongs to class pi on the basis of their immunological properties and N-terminal amino acid sequences. 4. The expression pattern of glutathione S-transferase isoenzymes in dog lens is different from that in pig, rat and bovine lenses.
Nishinaka
T
T
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Kodaka
R
R
Nanjo
H
H
Terada
T
T
Mizoguchi
T
T
Nishihara
T
T
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004285:Dogs; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007908:Lens, Crystalline / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity
D007527:Isoenzymes; D005982:Glutathione Transferase