PURIFICATION AND CHARACTERIZATION OF 25-HYDROXYVITAMIN D-3 1-ALPHA-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
Y. Nakamura et al., PURIFICATION AND CHARACTERIZATION OF 25-HYDROXYVITAMIN D-3 1-ALPHA-HYDROXYLASE FROM RAT-KIDNEY MITOCHONDRIA, FEBS letters, 419(1), 1997, pp. 45-48
Citations number
15
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
419
Issue
1
Year of publication
1997
Pages
45 - 48
Database
ISI
SICI code
0014-5793(1997)419:1<45:PACO2D>2.0.ZU;2-V
Abstract
We purified extensively 25-hydroxyvitamin D-3 1 alpha-hydroxylase (cal cidiol, 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 35 0-fold purification. Specific content of P450 was 1.1 nmol/mg of prote in and turnover number was 4.4 min(-1). (C) 1997 Federation of Europea n Biochemical Societies.