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Biochem J. 1995 Aug 15;310 ( Pt 1):353-8.

Sequencing and expression of a cDNA for human glutathione synthetase.

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Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra ACT.


A human brain cDNA clone encoding glutathione synthetase (EC has been sequenced and expressed in Escherichia coli. The protein is 474 amino acids in length with a subunit molecular mass of 52,352 Da. The recombinant protein exhibits glutathione synthetase activity and occurs as a homodimer. The recombinant glutathione synthetase was purified to homogeneity and had a specific activity of 1.73 mumol/min per mg of protein, an isoelectric point of 5.35 and a pH optimum between 7.0 and 7.5. Southern blots of human genomic DNA hybridized with the glutathione synthetase cDNA revealed a relatively simple pattern of strongly hybridizing fragments, indicating the absence of a large gene family and suggesting that there may be only one glutathione synthetase gene in the human genome.

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