Cytochrome P-450 in 7α-Hydroxylation of Taurodeoxycholic Acid

Dietmar Trülzsch; Helmut Greim; Peter Czygan; Ferenc Hutterer; Fenton Schaffner; Hans Popper; David Y. Cooper; Otto Rosenthal

doi:10.1021/bi00725a014

Cytochrome P-450 in 7_α-Hydroxylation of Taurodeoxycholic Acid

Dietmar Trülzsch
, Helmut Greim
, Peter Czygan
, Ferenc Hutterer
, Fenton Schaffner
, Hans Popper
, David Y. Cooper
, Otto Rosenthal

Mount Sinai School of Medicine
University of Pennsylvania

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Taurodeoxycholic acid is 7α hydroxylated to form taurocholic acid by rat liver microsomes in the presence of NADPH. This enzymatic reaction has a K_m of 0.03 mM. The reaction is inhibited by CO:O₂ mixtures with a K (Warburg's partition constant) of 0.5. The inhibition is maximally reversed by monochromatic light at the wavelength of 450 nm. These observations establish the P-450 dependence of 7α hydroxylation of taurodeoxycholic acid.

Original language	English
Pages (from-to)	76-79
Number of pages	4
Journal	Biochemistry
Volume	12
Issue number	1
DOIs	https://doi.org/10.1021/bi00725a014
State	Published - 1 Jan 1973
Externally published	Yes

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abstract = "Taurodeoxycholic acid is 7α hydroxylated to form taurocholic acid by rat liver microsomes in the presence of NADPH. This enzymatic reaction has a Km of 0.03 mM. The reaction is inhibited by CO:O2 mixtures with a K (Warburg's partition constant) of 0.5. The inhibition is maximally reversed by monochromatic light at the wavelength of 450 nm. These observations establish the P-450 dependence of 7α hydroxylation of taurodeoxycholic acid.",

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T1 - Cytochrome P-450 in 7α-Hydroxylation of Taurodeoxycholic Acid

AU - Trülzsch, Dietmar

AU - Greim, Helmut

AU - Czygan, Peter

AU - Hutterer, Ferenc

AU - Schaffner, Fenton

AU - Popper, Hans

AU - Cooper, David Y.

AU - Rosenthal, Otto

PY - 1973/1/1

Y1 - 1973/1/1

N2 - Taurodeoxycholic acid is 7α hydroxylated to form taurocholic acid by rat liver microsomes in the presence of NADPH. This enzymatic reaction has a Km of 0.03 mM. The reaction is inhibited by CO:O2 mixtures with a K (Warburg's partition constant) of 0.5. The inhibition is maximally reversed by monochromatic light at the wavelength of 450 nm. These observations establish the P-450 dependence of 7α hydroxylation of taurodeoxycholic acid.

AB - Taurodeoxycholic acid is 7α hydroxylated to form taurocholic acid by rat liver microsomes in the presence of NADPH. This enzymatic reaction has a Km of 0.03 mM. The reaction is inhibited by CO:O2 mixtures with a K (Warburg's partition constant) of 0.5. The inhibition is maximally reversed by monochromatic light at the wavelength of 450 nm. These observations establish the P-450 dependence of 7α hydroxylation of taurodeoxycholic acid.

UR - https://www.scopus.com/pages/publications/0015911781

U2 - 10.1021/bi00725a014

DO - 10.1021/bi00725a014

M3 - Article

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AN - SCOPUS:0015911781

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VL - 12

SP - 76

EP - 79

JO - Biochemistry

JF - Biochemistry

IS - 1

ER -

Cytochrome P-450 in 7_α-Hydroxylation of Taurodeoxycholic Acid

Abstract

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