Hydroxylation of taurolithocholate by isolated human liver microsomes II. Cytochrome P-450 dependency

P. Czygan; H. Greim; D. Trülzsch; J. Rudick; F. Hutterer; F. Schaffner; H. Popper; O. Rosenthal; D. Y. Cooper

doi:10.1016/0304-4165(74)90002-6

Hydroxylation of taurolithocholate by isolated human liver microsomes II. Cytochrome P-450 dependency

P. Czygan, H. Greim, D. Trülzsch, J. Rudick, F. Hutterer, F. Schaffner, H. Popper, O. Rosenthal, D. Y. Cooper

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Abstract

The conversion of taurolithocholate to taurohyodeoxycholate by 6α-hydroxylation by isolated human liver microsomes and NADPH is inhibited by CO and the inhibition is maximally reversedby monochromatic light at 450 nm indicating that the reaction is cytochrome P-450 dependent.

Original language	English
Pages (from-to)	168-171
Number of pages	4
Journal	Biochimica et Biophysica Acta - General Subjects
Volume	354
Issue number	2
DOIs	https://doi.org/10.1016/0304-4165(74)90002-6
State	Published - 4 Jul 1974
Externally published	Yes

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title = "Hydroxylation of taurolithocholate by isolated human liver microsomes II. Cytochrome P-450 dependency",

abstract = "The conversion of taurolithocholate to taurohyodeoxycholate by 6α-hydroxylation by isolated human liver microsomes and NADPH is inhibited by CO and the inhibition is maximally reversedby monochromatic light at 450 nm indicating that the reaction is cytochrome P-450 dependent.",

author = "P. Czygan and H. Greim and D. Tr{\"u}lzsch and J. Rudick and F. Hutterer and F. Schaffner and H. Popper and O. Rosenthal and Cooper, {D. Y.}",

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T1 - Hydroxylation of taurolithocholate by isolated human liver microsomes II. Cytochrome P-450 dependency

AU - Czygan, P.

AU - Greim, H.

AU - Trülzsch, D.

AU - Rudick, J.

AU - Hutterer, F.

AU - Schaffner, F.

AU - Popper, H.

AU - Rosenthal, O.

AU - Cooper, D. Y.

PY - 1974/7/4

Y1 - 1974/7/4

N2 - The conversion of taurolithocholate to taurohyodeoxycholate by 6α-hydroxylation by isolated human liver microsomes and NADPH is inhibited by CO and the inhibition is maximally reversedby monochromatic light at 450 nm indicating that the reaction is cytochrome P-450 dependent.

AB - The conversion of taurolithocholate to taurohyodeoxycholate by 6α-hydroxylation by isolated human liver microsomes and NADPH is inhibited by CO and the inhibition is maximally reversedby monochromatic light at 450 nm indicating that the reaction is cytochrome P-450 dependent.

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U2 - 10.1016/0304-4165(74)90002-6

DO - 10.1016/0304-4165(74)90002-6

M3 - Article

C2 - 4841343

AN - SCOPUS:0016194659

SN - 0304-4165

VL - 354

SP - 168

EP - 171

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

IS - 2

ER -

Hydroxylation of taurolithocholate by isolated human liver microsomes II. Cytochrome P-450 dependency

Abstract

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