STUDIES ON GLUTATHIONE S-TRANSFERASE IN HUMAN KIDNEY
Biochemical Characterization and Immunohistochemical Study in Human Embryonal Tissue
1985 Volume 76 Issue 8 Pages 1215-1225
Details
1985 Volume 76 Issue 8 Pages 1215-1225
Glutathione S-transferase (EC, 2, 5, 1, 18) was purified from human kidney. The purification was a four-step procedure; 105, 000G, 60min centrifugation of the homogenate, ammonium sulfate precipitation, DEAE cellulose, GSH-affinity column. The molecular weight of the subunit was calculated as 19, 000 by the relative mobility. The isoelectric point of the enzyme was 11.1 by the isoelectric focusing.
The human fetal tissue specimens from 5 to 12 weeks were stained by peroxidase antiperoxidase method (PAP) using the primary antibody obtained from an immunized rabbit. The enzyme staining was observed mainly in the liver, kidney and adrenal gland.
1) Diffuse staining of hepatic cells was already noted at 5 weeks, and remained to 12 weeks.
2) Metanephros was not stained before 7 weeks. After 8 weeks, the renal proximal tubles began to be stained.
3) The adrenal gland was stained in the fetal cortex at 5 weeks, and after 7 weeks strong stained nuclei were also observed in fetal cortical cells.
Special discussion was made on the glutathione S-transferase activity in the fetal adrenal cortex by referring to probable feto-specific steroidal metabolism.
