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Published on: January 7, 2013
Purification and characterization of 25-hydroxyvitamin D3 1alpha-hydroxylase from rat kidney mitochondria
Y Nakamura1, T A Eto, T Taniguchi
1Department 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.
