SOME INTERACTIONS OF STEROIDS, PYRIDINE NUCLEOTIDES AND ENZYMES

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Abstract
The rate of reduction of DPN by crystalline glutamic dehydrogenase is increased by the addition of corticosterone or progesterone at concentrations of 10−6 m or 10−8 m. The enzyme preparations were tested and found to be free of any transhydrogenase activity. No increase in rate could be demonstrated when these steroids were added to comparable systems of malic, lactic, or alcohol dehydrogenase, which transfer hydrogen to side 1 of the pyridine nucleotide, or with α-glycerophosphate or glyceraldehyde-3-phosphate dehydrogenase, which transfer hydrogen to side 2 of the pyridine nucleotide. Thionicotinamide DPN, but not TPN, 3-pyridine aldehyde DPN, deamino DPN, or 3-acetyl pyridine DPN, when substituted for DPN with glutamic dehydrogenase gave a system that responded to added steroids.

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