Literature DB >> 2328005

Separation of the cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3.

H Postlind1.   

Abstract

The cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3 have been separated. The cytochrome P-450 fractions required NADPH, mitochondrial ferredoxin and ferredoxin reductase for catalytic activity. The present report demonstrates that different forms of cytochrome P-450 are involved in 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3 and provides a basis for further purification and characterization of these enzymes.

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Year:  1990        PMID： 2328005     DOI： 10.1016/0006-291x(90)91702-t

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Antigenic and catalytic disparity in the distribution of cytochrome P-450-dependent 25-hydroxyvitamin D3-1 alpha- and 24-hydroxylases.

Authors:  K Takezawa; B Moorthy; M L Mandel; J C Garancis; J G Ghazarian
Journal:  Histochemistry       Date:  1990

2.  Characterization of mitochondrial cytochromes P-450 from pig kidney and liver catalysing 26-hydroxylation of 25-hydroxyvitamin D3 and C27 steroids.

Authors:  T Bergman; H Postlind
Journal:  Biochem J       Date:  1991-06-01       Impact factor: 3.857

3.  Liver mitochondrial cytochrome P450 CYP27 and recombinant-expressed human CYP27 catalyze 1 alpha-hydroxylation of 25-hydroxyvitamin D3.

Authors:  E Axén; H Postlind; H Sjöberg; K Wikvall
Journal:  Proc Natl Acad Sci U S A       Date:  1994-10-11       Impact factor: 11.205
  3 in total

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