help button home button Endocrine Society JCEM JCEM Call for Nominations for EIC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Submit a related Letter to the Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yoshida, K. I.
Right arrow Articles by Troen, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshida, K. I.
Right arrow Articles by Troen, P.

Journal of Clinical Endocrinology & Metabolism, Vol 50, 895-899, Copyright © 1980 by Endocrine Society

ARTICLES

Studies of the human testis. XIII. Properties of nicotinamide adenine dinucleotide (reduced form)-linked 17 alpha-hydroxylation

KI Yoshida, H Oshima and P Troen

A NADH-linked 17 alpha-hydroxylation of progesterone was examined using the washed microsome fraction prepared from human testes. The addition of NADP revealed no enhancement of 17 alpha-hydroxylation, indicating no transhydrogenation from NADH to NADP in the microsome fraction. The results further substantiate the presence of NADH-linked activity of 17 alpha-hydroxylation in addition to NADPH-linked activity. The Km of 17 alpha-hydroxylase for NADH was calculated as 4.3 x 10(-5) M at pH 7.4 and 37 C. The optimal pH of 17 alpha-hydroxylase was 7.7 in the presence of NADH and 7.9 in the presence of NADPH. An additive increase in the amount of product 17 alpha-hydroxyprogesterone was observed by adding NADH to the incubation medium containing an excess amount of NADPH. The data suggest that there are two distinct active sites for 17 alpha-hydroxylation. Furthermore, the inhibition of NADH-linked 17 alpha-hydroxylation by carbon monoxide indicates the involvement of cytochrome P450 in the electron transport system for the NADH-linked 17 alpha-hydroxylation.


This article has been cited by other articles:


Home page
 EndocrinologyHome page
J. K. Peterson, F. Moran, A. J. Conley, and I. M. Bird
Zonal Expression of Endothelial Nitric Oxide Synthase in Sheep and Rhesus Adrenal Cortex
Endocrinology, December 1, 2001; 142(12): 5351 - 5363.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1980 by The Endocrine Society