Purification and some properties of squalene-2,3-epoxide: lanosterol cyclase from rat liver.
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.
Kusano
M
M
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Abe
I
I
Sankawa
U
U
Ebizuka
Y
Y
D000818:Animals; D019751:Intramolecular Transferases; D007535:Isomerases / Q000302:isolation & purification*; D008099:Liver / Q000737:chemistry / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013552:Swine
D007535:Isomerases; D019751:Intramolecular Transferases; C021924:lanosterol synthase