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Partial purification of 2,3-oxidosqualene-lanosterol cyclase from hog-liver. Evidence for a functional thiol residue.

Authors
  • Duriatti, A1
  • Schuber, F
  • 1 Laboratoire de Chimie Enzymatique, CNRS UA 1182, Strasbourg, France.
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Mar 30, 1988
Volume
151
Issue
3
Pages
1378–1385
Identifiers
PMID: 3355560
Source
Medline
License
Unknown

Abstract

2,3-Oxidosqualene-lanosterol cyclase is an intrinsic microsomal protein which can be solubilized by ionic (deoxycholate) and nonionic (emulphogene) detergents with good yields. The hog-liver microsomal cyclase was purified approximately 140-fold by chromatography on DEAE-cellulose and hydroxylapatite. The partially purified enzyme was inactivated by N-ethylmaleimide, following pseudo-first order kinetics, indicating that a cysteine residue is essential for activity.

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