Abstract
THE triose (glyceraldehyde) dehydrogenase was studied by Green, Needham and Dewan1, who concluded from its distribution that it was a different enzyme from the triosephosphate dehydrogenase. We have succeeded in isolating and crystallizing the triose enzyme from rabbit skeletal muscle. After this was accomplished, we discovered that the crystals were in fact those of triosephosphate dehydrogenase. Their activity is actually some three hundred times greater with triosephosphate than with triose. It is therefore no longer necessary to assume the existence of triose dehydrogenase as a separate enzyme, as the two are identical.
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References
Green, D. E., Needham, D. M., and Dewan, J. G., Biochem. J., 31, 2327 (1937).
Warburg, O., and Christian, W., Biochem. Z., 303, 40 (1939).
Needham, D. M., and Pillai, R. K., Biochem. J., 31, 1837 (1937).
Needham, D. M., and Lu, G. D., Biochem. J., 32, 2040 (1938).
Cori, G. T., Slein, M. W., and Cori, C. F., J. Biol. Chem., 159, 565 (1945).
Bailey, K., Biol. Bull., 77, 303 (1939); Nature, 145, 934 (1940).
Baranowski, T., Z. physiol. Chem., 260, 43 (1939).
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Crystallization and Identity of the Triose and Triosephosphate Dehydrogenases of Muscle. Nature 156, 630–631 (1945). https://doi.org/10.1038/156630c0
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DOI: https://doi.org/10.1038/156630c0
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