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FEBS Lett. 1997 Dec 8;419(1):45-8.

Purification and characterization of 25-hydroxyvitamin D3 1alpha-hydroxylase from rat kidney mitochondria.

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1
Department of Surgery I, Miyazaki Medical College, Kiyotake, Japan.

Abstract

We purified extensively 25-hydroxyvitamin D3 1alpha-hydroxylase (calcidiol, NADPH: oxygen oxidoreductase (1-hydroxylating), EC 1.14.13.13) from kidney mitochondria of rachitic rats and disclosed its peculiar properties as a P450. The final preparation was identified as a 55 kDa protein having an intense absorption at 417 nm characteristic of P450. The specific activity was 4.8 nmol/min/mg of protein indicating a 350-fold purification. Specific content of P450 was 1.1 nmol/mg of protein and turnover number was 4.4 min-1.

PMID:
9426217
[Indexed for MEDLINE]
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