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Purification and characterization of glutathione S-transferase isozymes in dog lens
T Nishinaka1, R Kodaka, H Nanjo
1Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
The International Journal of Biochemistry
|November 1, 1992
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.