Regulation of hydroxylations in biosynthesis of bile acids: modulation of reconstituted 12 alpha-hydroxylase activity by protein fractions from rabbit liver cytosol and microsomes

Biochemical and Biophysical Research Communications
H DanielssonK Wikvall

Abstract

The activity of purified 12 alpha-hydroxylase from rabbit liver microsomes was modulated by including protein fractions from rabbit liver microsomes and cytosol into the system. The microsomal protein fraction stimulated 12 alpha-hydroxylation two times. The cytosolic fraction inhibited the reaction markedly. The microsomal 12 alpha-hydroxylase stimulatory activity was labile and the cytosolic 12 alpha-hydroxylase inhibitory activity was stable to mild heat treatment. Addition of ATP and MgCl2 or NaF had no effect on the activities of the two protein fractions. The activity of the microsomal stimulatory fraction decreased upon storage but could be reactivated by addition of reduced glutathione to the system.

References

Jan 1, 1975·Annual Review of Biochemistry·H Danielsson, J Sjövall
Oct 1, 1973·Biochemical and Biophysical Research Communications·C BernhardssonK Wikvall
May 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·L Spatz, P Strittmatter
Dec 15, 1981·Biochemical and Biophysical Research Communications·A SanghviR Lester
Dec 31, 1980·Biochemical and Biophysical Research Communications·H DanielssonK Wikvall

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Citations

Dec 2, 2006·European Journal of Drug Metabolism and Pharmacokinetics·S KevresanM Mikov
May 29, 1985·Biochimica Et Biophysica Acta·K Saarem, J I Pedersen
Jul 16, 2005·Gynecological Endocrinology : the Official Journal of the International Society of Gynecological Endocrinology·Bogusław CzernyZofia Myśliwiec
Mar 1, 1991·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Z R VlahcevicP B Hylemon
Sep 8, 2005·Menopause : the Journal of the North American Menopause Society·Bogusław CzernyAndrzej Pawlik
Sep 15, 1984·Biochemical Pharmacology·S Andersson, H Boström

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