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

Shin Ichi Hayashi, Emiko Usui, Kyuichiro Okuda

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25 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)863-866
Number of pages4
JournalJournal of biochemistry
Issue number5
Publication statusPublished - 1988 May
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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