Purification and characterization of 7β-hydroxysteroid dehydrogenase from rabbit liver microsomes

2004 ◽  
Vol 91 (3) ◽  
pp. 185-190 ◽  
Author(s):  
Hironori Shiotsuki ◽  
Yorio Maeda ◽  
Kazuo Chijiiwa
Keyword(s):  
Liver Microsomes ◽  
Hydroxysteroid Dehydrogenase ◽  
Rabbit Liver ◽  
Purification And Characterization

Purification and characterization of 3ß-hydroxysteroid dehydrogenase from rat and rabbit liver microsomes

1994 ◽  
Vol 1 ◽  
pp. 167
Author(s):  
Y. Maeda ◽  
Y. Ando ◽  
H. Nagatomo ◽  
S. Tateno ◽  
S. Higashi ◽  
...  
Keyword(s):  
Liver Microsomes ◽  
Hydroxysteroid Dehydrogenase ◽  
Rabbit Liver ◽  
Purification And Characterization

scholarly journals A 17 β-hydroxysteroid dehydrogenase of female rabbit liver cytosol. Purification and characterization of multiple forms of the enzyme

1985 ◽  
Vol 225 (2) ◽  
pp. 383-390 ◽  
Author(s):  
G R Antoun ◽  
I Brglez ◽  
D G Williamson
Keyword(s):  
Dehydrogenase Activity ◽  
Quaternary Structure ◽  
Hydroxysteroid Dehydrogenase ◽  
Rabbit Liver ◽  
Multiple Forms ◽  
Purification And Characterization ◽  
Enzyme Form ◽  
Female Rabbit ◽  
Androstane Series

Multiple forms of the soluble 17 beta-hydroxysteroid dehydrogenase of female rabbit liver were identified. NAD-dependent and NADP-dependent enzyme activities were separated by affinity chromatography on agarose-immobilized Procion Red HE3B, and three forms of the NADP-dependent enzyme activity were purified by chromatofocusing. These three enzyme forms are charge isomers and have no quaternary structure. The enzymes catalysed the C-17 oxidoreduction of oestrogens and androgens; with all enzyme forms the activity towards androgens was higher than that toward oestrogens. The enzymes also exhibited 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. Comparison of the relative activities of the enzymes towards a number of oestrogen and androgen substrates revealed differences among the enzyme forms for both the oxidative and the reductive reactions. In particular, one enzyme form had a significantly lower Km for the 3 alpha-hydroxysteroid substrate and a higher 3 alpha-/17 beta-hydroxysteroid dehydrogenase activity ratio than the other two enzyme forms.

Purification and characterization of a form of cytochrome P450 from bear liver microsomes

1995 ◽  
Vol 49 (7) ◽  
pp. 965-970 ◽  
Author(s):  
Yukio Yamamoto ◽  
Makihiko Masuda ◽  
Akio Kazusaka ◽  
Susumu Imaoka ◽  
Yoshihiko Funae ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Liver Microsomes ◽  
Purification And Characterization
Sign in / Sign up

Export Citation Format

Share Document