Enzymatic sulfation of glycochenodeoxycholic acid by tissue fractions from adult hamsters.

Abstract:

:Using a radiometric assay with glycochenodeoxycholic acid as substrate, bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase activity was found in 105,000 g supernatant fractions of liver, proximal intestine, and adrenal gland homogenates from adult hamsters. Optimum conditions for measurement of the hepatic enzyme were determined. In both male and female animals sulfation only occurred at the 7 alpha-position. Saturation analysis with glycohenodeoxycholic acid revealed that the higher activity observed in fractions from female compared to male hamsters was due to a 4-fold lower apparent Km (79 muM vs. 317 muM) for this bile acid in the females. The sulfation of glycohenodeoxycholic acid was competitively inhibited by glycolithocholic acid, chenodeoxycholic acid, and ursodeoxycholic acid. The data are consistent with the concept that sulfation of many, if not all, bile acids can occur in vivo.

journal_name

J Lipid Res

authors

Barnes S,Burhol PG,Zander R,Haggstrom G,Settine RL,Hirschowitz BI

subject

Has Abstract

pub_date

1979-11-01 00:00:00

pages

952-9

issue

8

eissn

0022-2275

issn

1539-7262

journal_volume

20

pub_type

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