Abstract
The succinate and glycerophosphate dehydrogenases belong to the group of ‘cytoehrome-reducing dehydrogenases’1. In some tissues the succinic system is by far the more active, but in others (for example, rabbit skeletal muscle) the two systems are equally important. Hopkins et al.2 suggested that in the succinoxidase system from heart muscle there was an intermediate factor linking the dehydrogenase with cytoehrome c. Stern and Melnick3 claimed to have separated the factor, although their evidence has been rightly questioned4. Straub5 has shown that an oxidase preparation lacking the factor can be reactivated by a heart-muscle dispersion in which the succinic dehydrogenase and cytoehrome oxidase have been destroyed. Experiments reported below show the existence in liver of a soluble factor which links or makes accessible the succinodehydrogenase to the cytoehrome system. This factor or activator is not necessary for the α-glycerophosphate system.
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References
Green, D. E., and Brosteaux, J., Biochem. J., 30, 1489 (1936).
Hopkins, F. G., Lutwak-Mann, C., and Morgan, E. J., Nature, 143, 556(1939).
Stern, K. G., and Melnick, J. L., Nature, 144, 330 (1939).
Keilin, D., and Hartree, E. F., Proc. Roy. Soc., B, 129, 277 (1940).
Straub, F. B., Z. physiol. Chem., 272, 219 (1941).
Quastel, J. H., and Wheatley, A. H. M., Biochem. J. 32, 936 (1938).
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STOPPANI, A. Constitution of the Succinate and α-Glycerophosphate Oxidase Systems. Nature 160, 52–53 (1947). https://doi.org/10.1038/160052a0
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DOI: https://doi.org/10.1038/160052a0
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