title: Purification and some properties of squalene-2,3-epoxide: lanosterol cyclase from rat liver.
abstract: Squalene-2,3-epoxide: lanosterol cyclase was purified from rat liver in five steps as a soluble and homogeneous protein. The purified enzyme showed a single band on SDS-polyacrylamide gel electrophoresis with a molecular weight of 75 kD. In its native state it behaved as a homo-dimer. The isoelectric point of 5.5 and the apparent Km value for (3S)-squalene-epoxide of 55 microM were estimated for the cyclase.
authors.affiliation: Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Kusano
authors.forename: I
authors.initials: I
authors.lastname: Abe
authors.forename: U
authors.initials: U
authors.lastname: Sankawa
authors.forename: Y
authors.initials: Y
authors.lastname: Ebizuka
mesh_terms: D000818:Animals; D019751:Intramolecular Transferases; D007535:Isomerases / Q000302:isolation & purification*; D008099:Liver / Q000737:chemistry / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013552:Swine
chemical_list: D007535:Isomerases; D019751:Intramolecular Transferases; C021924:lanosterol synthase