Purification and some properties of squalene-2,3-epoxide: lanosterol cyclase from rat liver

Chem Pharm Bull (Tokyo). 1991 Jan;39(1):239-41. doi: 10.1248/cpb.39.239.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Intramolecular Transferases*
  • Isomerases / isolation & purification*
  • Liver / chemistry
  • Liver / enzymology*
  • Rats
  • Rats, Inbred Strains
  • Swine

Substances

  • Isomerases
  • Intramolecular Transferases
  • lanosterol synthase