Purification of rat liver microsomal glutathione transferase.
The rat liver microsomal glutathione transferase was activated by N-ethylmaleimide, solubilized by Triton X-100 and purified by chromatography on hydroxyapatite and CM Sephadex C-50. A 28-fold purification resulted in a 38% yield. The purified protein moved as a band with an apparent molecular weight of 14,000 on sodium dodecyl sulphate polyacrylamide gel electrophoresis and appeared to be nearly homogeneous. The N-terminal amino acid of the purified enzyme was alanine, identified by the dansyl method. Optimum pH and temperature were 6.8 and 30 degrees C, respectively.
Shi
N A
NA
Department of Environmental Toxicology, Tongji Medical University, Wuhan.
Liu
Y G
YG
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D005982:Glutathione Transferase