(I) affinity labelling of an histidine of the active site of the human placental 17β‐oestradiol dehydrogenase
- 19 October 1973
- journal article
- Published by Wiley in FEBS Letters
- Vol. 36 (1), 23-26
- https://doi.org/10.1016/0014-5793(73)80328-x
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- (II) Enhancement of the catalytic activity of the human placental 17 β‐oestradiol dehydrogenase by carboxymethylation of an histidyl residue of the active siteFEBS Letters, 1973
- Affinity labelling of the active site of the 17β‐oestradiol dehydrogenase of human placental cytosolFEBS Letters, 1973
- Human placental 17β‐oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteineFEBS Letters, 1973
- Amino acid composition and subunit structure. Human placental 17β-estradiol dehydrogenaseBiochemistry, 1972
- Affinity chromatography: Large‐scale purification of the soluble oestradiol‐17‐β dehydrogenase of human placentaFEBS Letters, 1972
- Soluble 17β-hydroxysteroid dehydrogenase from human placenta. Evidence for a subunit structureBiochemistry, 1971
- The subunit structure of human placental 17β-estradiol dehydrogenaseBiochemical and Biophysical Research Communications, 1971
- Reaction Mechanism of 17β-Estradiol Dehydrogenase Determined by Equilibrium Rate ExchangePublished by Elsevier ,1971
- Horse Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1970