Affinity radiolabeling identifies peptides and amino acids associated with substrate binding in human placental 3 beta-hydroxy-delta(5)-steroid dehydrogenase.-Reference-Cited by-同舟云学术

Affinity radiolabeling identifies peptides and amino acids associated with substrate binding in human placental 3 beta-hydroxy-delta(5)-steroid dehydrogenase.

Published:1993-09 Issue:25 Volume:268 Page:18507-18512
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Thomas J.L.,Nash W.E.,Myers R.P.,Crankshaw M.W.,Strickler R.C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference25 articles.

1. Human placental Δ5-3β hydroxysteroid dehydrogenase activity (Δ5-33 HSDH): Intracellular distribution, kinetic properties, retroinhibition and influence of membrane delipidation

2. Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5 → 4-ene-isomerase: Purification from microsomes, substrate kinetics, and inhibition by product steroids

3. Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5→ 4-ene-isomerase: Purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes

4. Purification and properties of testicular 3β-hydroxy-5-ene-steroid dehydrogenase and 5-ene-4-ene isomerase

5. Purification and characterization of rat adrenal 3β-hydroxysteroid dehydrogenase with steroid 5-ene-4-ene-isomerase

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