Purification and characterization of glutathione S-transferase isozymes in dog lens.

Nishinaka T, Kodaka R, Nanjo H, Terada T, Mizoguchi T, Nishihara T

Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.

Int J Biochem. 1992 Nov;24(11):1737-42. doi: 10.1016/0020-711x(92)90122-h.

Abstract

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.

摘要