Partial purification of 2,3-oxidosqualene-lanosterol cyclase from hog-liver. Evidence for a functional thiol residue.
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.
Duriatti
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Laboratoire de Chimie Enzymatique, CNRS UA 1182, Strasbourg, France.
Schuber
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F
D000818:Animals; D003840:Deoxycholic Acid / Q000494:pharmacology; D005033:Ethylmaleimide / Q000494:pharmacology; D019751:Intramolecular Transferases; D007535:Isomerases / Q000032:analysis / Q000302:isolation & purification*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D012995:Solubility; D013438:Sulfhydryl Compounds / Q000032:analysis*; D013552:Swine
D013438:Sulfhydryl Compounds; D003840:Deoxycholic Acid; D007535:Isomerases; D019751:Intramolecular Transferases; C021924:lanosterol synthase; D005033:Ethylmaleimide