The Activation of the Δ5-3-Keto Steroid Isomerase in Rat Adrenal Small Particles by Diphosphopyridine Nucleotides*
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00866a045
Reference13 articles.
1. Treatment of Enzyme Kinetic Data
2. The Preparation and Properties of Crystalline Δ5-3-Ketosteroid Isomerase
3. The Conversion of Pregnenolone to Progesterone by Small Particles from Rat Adrenal*
4. The Δ5-3β-hydroxysteroid dehydrogenase of bovine corpus luteum and adrenal
5. Δ5 -3-Keto isomerases — specificity and inhibition studies in bovine adrenal homogenate fractions and distribution in rat tissues
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1. Analysis of coenzyme binding by human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5→4-ene-isomerase using 5′-[p-(fluorosulfonyl)benzoyl]adenosine, an affinity labeling cofactor analog;The Journal of Steroid Biochemistry and Molecular Biology;1991-10
2. 3.beta.-Hydroxy-.DELTA.5-steroid dehydrogenase/3-keto-.DELTA.5-steroid isomerase from bovine adrenals: mechanism of inhibition by 3-oxo-4-aza steroids and kinetic mechanism of the dehydrogenase;Biochemistry;1989-01-10
3. Activation of human placental 5-pregnene-3,20-dione isomerase activity by pyridine nucleotides;Journal of Steroid Biochemistry;1988-05
4. Testicular and adrenal 3β-hydroxy-5-ene-steroid dehydrogenase and 5-ene-4-ene isomerase;Journal of Steroid Biochemistry;1987-01
5. Purification and characterization of rat adrenal 3β-hydroxysteroid dehydrogenase with steroid 5-ene-4-ene-isomerase;Journal of Steroid Biochemistry;1986-03
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