Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione.-Reference-Cited by-同舟云学术

Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione.

Published:1983-10 Issue:19 Volume:258 Page:11460-11464
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Murdock G L,Chin C C,Offord R E,Bradshaw R A,Warren J C

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference19 articles.

1. Purification of estradiol-17β dehydrogenase from human placenta by affinity chromatography

2. Crystallization of human placental estradiol 17beta-dehydrogenase. A new method for crystallizing labile enzymes.

3. Synthesis of 16alpha-bromoacetoxyestradiol 3-methyl ether and study of the steroid binding site of human placental estradiol 17beta-dehydrogenase.

4. Isolation of histidyl peptides of the steroid-binding site of human placental estradiol 17β-dehydrogenase

5. Synthesis of 4-bromoacetamidoestrone methyl ether and study of the steroid binding site of human placental estradiol 17beta-dehydrogenase.

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