The affinity alkylators, 11α-bromoacetoxyprogesterone and estrone 3-bromoacetate, modify a common histidyl residue in the active site of human placental 17β,20α-hydroxysteroid dehydrogenase
- 1 July 1986
- journal article
- research article
- Published by Elsevier in The Journal of Steroid Biochemistry and Molecular Biology
- Vol. 25 (1) , 103-108
- https://doi.org/10.1016/0022-4731(86)90287-6
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Reactivation of human placental 17.beta.,20.alpha.-hydroxysteroid dehydrogenase affinity alkylated by estrone 3-(bromoacetate): topographic studies with 16.alpha.-(bromoacetoxy)estradiol 3-(methyl ether)Biochemistry, 1985
- Reactivation of human placental 17β, 20α-hydroxysteroid dehydrogenase: Affirmation of affinity labeling principlesSteroids, 1984
- Isolation of histidyl peptides of the steroid-binding site of human placental estradiol 17β-dehydrogenaseSteroids, 1982
- Affinity labeling of human placental 17.beta.-estradiol dehydrogenase and 20.alpha.-hydroxysteroid dehydrogenase with 5'-[p-(fluorosulfonyl)benzoyl]adenosineBiochemistry, 1981
- Estradiol 17β-dehydrogenase and 20α-hydroxysteroid dehydrogenase from human placental cytosol: one enzyme with two activities?Steroids, 1980
- Some new developments in the knowledge of human placental estradiol-17β dehydrogenaseJournal of Steroid Biochemistry, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Synthesis of 21-acryloxyprogesterone, 21-bromoacetoxyprogesterone and 11α-bromoacetoxyprogesterone for affinity labelingBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1972
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934