Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 1997 Dec 8;419(1):45-8.

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

Author information

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


We purified extensively 25-hydroxyvitamin D3 1alpha-hydroxylase (calcidiol, NADPH: oxygen oxidoreductase (1-hydroxylating), EC 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.

[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center