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Biochem Mol Biol Int. 1993 Aug;30(6):1053-60.

Purification and biochemical characterization of gamma-glutamylcysteine synthetase from a human malignant astrocytoma cell line.

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Department of Experimental Pediatrics, University of Texas M.D. Anderson Cancer Center, Houston 77030.


gamma-Glutamylcysteine synthetase (EC the key regulatory enzyme in glutathione biosynthesis was purified from a human malignant astrocytoma cell line using a combination of ammonium sulfate fractionation, DE-52 cellulose chromatography and ATP-agarose affinity chromatography. The purified protein had a specific activity of 1725 units/mg protein, which represented an 86-fold purification and a 22% yield. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed two major subunits with apparent molecular sizes of 72 kDa and 32 kDa. The Km values for L-glutamate and L-alpha-aminobutyrate were 0.03 mM and 0.14 mM respectively. These molecular and catalytic properties of gamma-glutamylcysteine synthetase from astrocytoma cell line are similar, but not identical to those purified from rat kidney.

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