Immunoaffinity purification of aromatase cytochrome P-450 from human placental microsomes, metabolic switching from aromatization to 1β and 2β-monohydroxylation, and recognition of aromatase isozymes-Reference-Cited by-同舟云学术

Immunoaffinity purification of aromatase cytochrome P-450 from human placental microsomes, metabolic switching from aromatization to 1β and 2β-monohydroxylation, and recognition of aromatase isozymes

Published:1987-07 Issue:1-3 Volume:50 Page:11-28
ISSN:0039-128X
Container-title:Steroids
language:en
Short-container-title:Steroids

Author:

Osawa Yoshio,Yoshida Nobutake,Fronckowiak Mary,Kitawaki Jo

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Pharmacology,Endocrinology,Molecular Biology,Biochemistry

Reference34 articles.

1. The involvement of human placental microsomal cytochrome P-450 in aromatization;Thompson;J Biol Chem,1974

2. Solubilization of estrogen synthetase from human term placental microsomes using detergents;Bellino;J Steroid Biochem,1978

3. Solubilization of androgen binding protein responsible for estrogen biosynthesis from lyophilized 900G particulates of human term placenta;Osawa,1978

4. Isolation of human placental cytochrome P-450 and its mechanism of action of androgen aromatization;Osawa,1980

5. Multiple forms of aromatase and response to breast cancer aromatase to antiplacental aromatase II antibodies;Osawa;Cancer Res (Supl),1982

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