Summary
In gerbil adrenal cortex the activity of intramitochondrial NADP-linked isocitric dehydrogenase (IDH) is up to 10-fold greater than the NAD-linked IDH. The NADP-IDH, apparent Km 0.58 mM, Vmax 280 nmoles/min/mg mitochondrial protein, appears to be the major source of reducing equivalents to support adrenal mitochondrial steroid 11B- and 19-hydroxylation in this species.
References
Simpson, E. R., and Waterman, M. R., Can. J. Biochem. Cell Biol.61 (1983) 692.
Purvis, J. L., Battu, R. G., and Peron, F. G., in: Functions of the Adrenal Cortex, vol. 2, p. 1007.Ed. K. McKerns. Appelton, New York 1968.
Simpson, E. R., Cooper, D. Y., and Estabrook, R. W., Recent Prog. Horm. Res.25 (1969) 523.
Oliver, J. T., and Peron, F. G., Steroids4 (1964) 351.
McCarthy, J. L., and Dickinson, A., Proc. Soc. exp. Biol. Med.165 (1980) 69.
Bradford, M. R., Analyt. Biochem.72 (1976) 248.
McCarthy, J. L., Kramer, R., Waterman, M. R., and Simpson, E. R., Archs Biochem. Biophys.222 (1983) 590.
Peron, F. G., and McCarthy, J. L., in: Functions of the Adrenal Cortex, vol. 1, p. 261. Ed. K. McKerns. Appelton, New York, 1968.
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McCarthy, J.L., Gauthier, J. NADP-isocitric dehydrogenase of gerbil adrenal mitochondria: Support of steroid hydroxylation. Experientia 41, 484–485 (1985). https://doi.org/10.1007/BF01966160
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DOI: https://doi.org/10.1007/BF01966160