The inhibition of 3α-hydroxy steroid-activated nicotinamide-adenine dinucleotide (phosphate) transhydrogenase by some antimetabolic compounds
- 1 April 1964
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 91 (1) , 76-81
- https://doi.org/10.1042/bj0910076
Abstract
This work establishes the inhibition in vitro of the 3a-hydroxy steroid-activated NAD(P)-transhydrogenating enzyme system from rat liver by certain derivatives of purines and pyrimidines. Of the compounds tested the most active purine and pyrimidine analogues appear to be those having a high therapeutic index against experimental cancer. The inhibition produced is additive as between purines and pyrimidines and also between inhibitory steroid hormones and the antimetabolites.This publication has 7 references indexed in Scilit:
- Purification and properties of the 3α-hydroxy steroid-dependent nicotinamide-adenine dinucleotide transhydrogenase of rat liverBiochemical Journal, 1963
- PURIFICATION OF 17BETA-HYDROXYSTEROID DEHYDROGENASE OF HUMAN PLACENTA AND STUDIES ON ITS TRANSHYDROGENASE FUNCTION1962
- Antagonists Of Purine And Pyrimidine Metabolites And Of Folk AcidAdvances in Cancer Research, 1962
- Inhibition of 3 α-hydroxysteroid-mediated transhydrogenase of rat-liver homogenate by Δ4-3-oxosteroidsBiochimica et Biophysica Acta, 1960
- SEPARATION OF HUMAN PLACENTAL ESTROGEN-SENSITIVE TRANSHYDROGENASE FROM ESTRADIOL-17-BETA DEHYDROGENASE1959
- 3α-Hydroxysteroids as Coenzymes of Hydrogen Transfer between Di- and Triphosphopyridine NucleotidesJournal of Biological Chemistry, 1958
- Estradiol-sensitive isocitric dehydrogenase in noncancerous and cancerous human breast tissueCancer, 1958