RGD Reference Report - Purification and characterization of 25-hydroxyvitamin D3 1alpha-hydroxylase from rat kidney mitochondria. - Rat Genome Database

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

Authors: Nakamura, Y  Eto, TA  Taniguchi, T  Miyamoto, K  Nagatomo, J  Shiotsuki, H  Sueta, H  Higashi, S  Okuda, KI  Setoguchi, T 
Citation: Nakamura Y, etal., FEBS Lett. 1997 Dec 8;419(1):45-8.
RGD ID: 2307316
Pubmed: PMID:9426217   (View Abstract at PubMed)

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.

Objects referenced in this article
Gene Cyp27b1 cytochrome P450, family 27, subfamily b, polypeptide 1 Rattus norvegicus

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