Purification of cytochrome P-450D1α (25-hydroxyvitamin D3-1α-hydroxylase) of bovine kidney mitochondria

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Summary

Cytochrome P-450D1α purified from bovine renal mitochondria was electrophoretically homogeneous and gave a single protein band. The cytochrome P-450D1α is an immunochemical possessing properties in common with the mitochondrial cytochrome P-450's of other tissues. The 1α-hydroxylase system of 25-hydroxyvitamin D3 was reconstituted with the cytochrome P-450D1α, NADPH-renoredoxin reductase and renoredoxin, each component being essential to the lα-hydroxylase system. The substrate specificity of the cytochrome P-450D1α was investigated.

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