Purification of rat liver microsomal glutathione transferase
Shi Nian , Liu Yu-gu
Current Medical Science ›› 1991, Vol. 11 ›› Issue (3) : 182 -186.
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 14000 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°C, respectively.
microsomal glutathione transferase / liver / purification
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