Abnormal γ-glutamylcysteine synthetase activities in sheep red blood cells
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Abstract
Red blood cell γ-glutamylcysteine synthetase (GC-S) activities and glutathione (GSH) concentrations were investigated in pure-bred Finnish Landrace, Tasmanian Merino, and Finnish Landrace × Tasmanian Merino sheep Previous studies were confirmed that a dominant gene (L) at the GSH locus leads to partial GC-S and GSH deficiency, while a recessive gene (h) at the Tr locus codes for defective red cell amino acid transport, concomitant GSH deficiency, and significantly elevated levels of GC-S. In addition, new results are presented which suggest that there is a dominant gene (A) at another locus distinct from GSH and Tr (provisionally designated GC-S) which has a marked epistatic enhancing effect on measured GC-S activities.
Key words
γ-glutamylcysteine synthetase glutathione sheep erythrocytePreview
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References
- Beutler, E., Duron, O., and Kelly, B. M. (1963). Improved method for the determination of blood glutathione. J. Lab. Clin. Med. 61882.Google Scholar
- Board, P. G., Morris, R. J. H., and Peter, D. W. (1976). The enzymes of glutathione synthesis in erythrocytes from GSH-high and GSH-low type Australian Merino sheep. Int. J. Biochem. 7381.Google Scholar
- Board, P. G., Smith, J. E., Moore, K., and Ou, D. (1980). Erythrocyte γ-glutamylcysteine synthetase from normal and low-glutathione sheep. Biochim. Biophys. Acta 613534.Google Scholar
- Eagleton, G. E., Hall, J. G., and Russell, W. S. (1970). Am estimation of dominance at the locus controlling blood potassium in sheep. Anim. Blood Groups Biochem. Genet. 1135.Google Scholar
- Ellory, J. C., Tucker, E. M., and Deverson, E. V. (1972). The identification of ornithine and lysine at high concentrations in the red cells of sheep with an inherited deficiency of glutathione. Biochim. Biophys. Acta 279481.Google Scholar
- Larsson, A. (1981). 5-Oxoprolinuria and other inborn errors related to the γ-glutamyl cycle. In Belton, N. R., and Toothill, C. (eds.), Transport in Inherited Disease MIT Press, Lancaster, p. 277.Google Scholar
- Minnich, V., Smith, M. B., Brauner, M. J., and Majerus, P. W. (1971). Glutathione biosynthesis in human erythrocytes. 1. Identification of the enzymes of glutathione synthesis in haemolysates. J. Clin. Invest. 50507.Google Scholar
- Paniker, N. V., and Beutler, E. (1972). The effect of methylene blue and diaminodiphenylsulfone on red cell reduced glutathione synthesis. J. Lab. Clin. Med. 80481.Google Scholar
- Smith, J. E. (1973). Concentrations of glutathione precursors in erythrocytes of normal and glutathione-deficient sheep. Am. J. Vet. Res. 34591.Google Scholar
- Tucker, E. M., Kilgour, L., and Young, J. D. (1976). The genetic control of red cell glutathione deficiencies in Finnish Landrace and Tasmanian Merino sheep and in crosses between these breeds. J. Agr. Sci. Camb. 87315.Google Scholar
- Young, J. D., and Nimmo, I. A. (1975). GSH biosynthesis in glutathione-deficient erythrocytes from Finnish Landrace and Tasmanian Merino sheep. Biochim. Biophys. Acta 404132.Google Scholar
- Young, J. D., and Tucker, E. M. (1982). Erythrocyte glutathione deficiency in sheep. In Proceedings of the Fifth Karolinska Institute Nobel Conference—Functions of Glutathione, Biochemical, Physiological and Toxicological Aspects Raven Press, New York (in press).Google Scholar
- Young, J. D., Nimmo, I. A., and Hall, J. G. (1975). The relationship between GSH, GSSG and non-GSH thiol in GSH-deficient erythrocytes from Finnish Landrace and Tasmanian Merino sheep. Biochim. Biophys. Acta 404124.Google Scholar
- Young, J. D., Ellory, J. C., and Tucker, E. M. (1976). Amino acid transport in normal and glutathione-deficient sheep erythrocytes. Biochem. J. 15443.Google Scholar
- Young, J. D., Tucker, E. M., and Kilgour, L. (1982). Genetic control of amino acid transport in sheep erythrocytes. Biochem. Genet. 20723.Google Scholar
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© Plenum Publishing Corporation 1983