PMID: 5257956May 1, 1969Paper

Some properties of the microsomal 2,3-oxidosqualene sterol cyclase

Proceedings of the National Academy of Sciences of the United States of America
S YamamotoK Bloch

Abstract

The transformation of 2,3-oxidosqualene to lanosterol is catalyzed by a microsomal enzyme (cyclase) which can be obtained in soluble and partially purified form by treatment of liver microsomes with deoxycholate as previously shown. The catalytic and physical properties of the soluble enzyme are determined by ionic strength. In 0.4 M KCl the cyclase exists largely in a dissociated, enzymatically active form. Solutions of low ionic strength (0.1 M KCl or less) cause enzyme aggregation and loss of activity. The anionic detergent deoxycholate is essential for cyclase activity, but is effective only in a narrow concentration range.

Citations

Jul 2, 1973·Biochemical and Biophysical Research Communications·R C Johnson, S N Shah
Dec 16, 1970·Biochimica Et Biophysica Acta·I ShechterK Bloch
Aug 15, 1985·Archives of Biochemistry and Biophysics·N T NashedD M Jerina
Mar 30, 1988·Biochemical and Biophysical Research Communications·A Duriatti, F Schuber
Sep 12, 2016·Current Hypertension Reports·Rossella IatrinoLaura Zagato
Nov 25, 1998·Critical Reviews in Biochemistry and Molecular Biology·L Cattel, M Ceruti
Jul 1, 1974·Journal of Neurochemistry·R G Dennick, P D Dean
Jan 2, 1976·European Journal of Biochemistry·G T Phillips, K H Clifford
Mar 31, 2021·Journal of Lipid Research·Kei Yamamoto, Natsuo Ueda
Apr 24, 2002·Biochemical and Biophysical Research Communications·Teruo Ono

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