Sex-related difference in vitamin D3 25-hydroxylase of rat liver microsomes.

Abstract:

:Cholecalciferol 25-hydroxylase was partially purified by polyethylene glycol fractionation and chromatographies on octylamino-Sepharose and hydroxylapatite columns starting from the liver microsomes of female rats, and compared with P-450cc25 purified from the liver microsomes of male rats (Hayashi, et al. (1986) J. Biochem. 99, 1753-1763). On octylamino-Sepharose 4B column chromatography, most of the activity was recovered in the fraction eluted with 0.08% Emulgen 913 in the case of the male enzyme, whereas the female enzyme was recovered in the fraction eluted with 0.2% Emulgen. Anti-cc25 antibodies against purified male P-450cc25 inhibited the 25-hydroxylation activity of male polyethylene glycol (PEG) fraction and partially purified male enzyme, but did not inhibit the activities of the corresponding female fractions. The antibodies formed a single precipitation line with male P-450cc25, but did not form a precipitation line with partially purified female 25-hydroxylase on immuno-diffusion. These observations indicated that the vitamin D3 25-hydroxylase in female rat liver microsomes is a different entity from that of male rats.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hayashi S,Usui E,Okuda K

doi

10.1093/oxfordjournals.jbchem.a122362

subject

Has Abstract

pub_date

1988-05-01 00:00:00

pages

863-6

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

103

pub_type

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