1. Purification and characterization of glutathione S-transferase isozymes in dog lens.
- Author
-
Nishinaka T, Kodaka R, Nanjo H, Terada T, Mizoguchi T, and Nishihara T
- Subjects
- Amino Acid Sequence, Animals, Blotting, Western, Dogs, Glutathione Transferase isolation & purification, Humans, Isoelectric Point, Isoenzymes isolation & purification, Molecular Sequence Data, Molecular Weight, Substrate Specificity, Glutathione Transferase metabolism, Isoenzymes metabolism, Lens, Crystalline enzymology
- Abstract
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.
- Published
- 1992
- Full Text
- View/download PDF