Purification and characterization of 25‐hydroxyvitamin D3 1α‐hydroxylase from rat kidney mitochondria

FEBS Letters

Shiotsuki, Hironori¹  Miyamoto, Koji¹  Nagatomo, Junji¹  Eto, Tada-Aki¹  Higashi, Shushi¹  Nakamura, Yoshito¹  Setoguchi, Toshiaki¹  Sueta, Hideto¹  Taniguchi, Tomotaka¹  Okuda, Kyu-Ichiro¹ 

[1] Department of Surgery I, Miyazaki Medical College, Kiyotake, Miyazaki 889-16, Japan

关键词: 25-Hydroxyvitamin D3;    1α-Hydroxylase;    P450;    CHAPS;    Rat kidney;    DTT;    dithiothreitol;    CHAPS;    3[(3-cholamidopropyl)-dimethylammonio]1-propanesulfonate;    PEG;    polyethylene glycol;   

DOI  :  10.1016/S0014-5793(97)01432-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We purified extensively 25-hydroxyvitamin D₃ 1α-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.

【 授权许可】

Unknown