Soluble 17β-hydroxysteroid dehydrogenase from human placenta. Evidence for a subunit structure
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00797a005
Reference21 articles.
1. A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis
2. Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins
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1. Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Human Estrogenic 17β-Hydroxysteroid Dehydrogenase: Predominance of Estrone Reduction and Its Induction by NADPH;Biochemical and Biophysical Research Communications;1999-06
3. Human placental estradiol 17β-dehydrogenase: structural and catalytic changes during urea denaturation;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-10
4. Human 17β-hydroxysteroid dehydrogenase: optical properties of its complex with NADP+;The Journal of Steroid Biochemistry and Molecular Biology;1995-01
5. Crystal growth of human estrogenic 17β-hydroxysteroid dehydrogenase;Acta Crystallographica Section D Biological Crystallography;1994-07-01
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