Literature DB >> 2049810

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

M Kusano1, I Abe, U Sankawa, Y Ebizuka.   

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.

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Year:  1991        PMID: 2049810     DOI: 10.1248/cpb.39.239

Source DB:  PubMed          Journal:  Chem Pharm Bull (Tokyo)        ISSN: 0009-2363            Impact factor:   1.645


  3 in total

1.  Identification of the active site of vertebrate oxidosqualene cyclase.

Authors:  I Abe; G D Prestwich
Journal:  Lipids       Date:  1995-03       Impact factor: 1.880

2.  3-Carboxy-4-nitrophenyl-dithio-1,1',2-trisnorsqualene: a site-directed inactivator of yeast oxidosqualene cyclase.

Authors:  G Balliano; G Grosa; P Milla; F Viola; L Cattel
Journal:  Lipids       Date:  1993-10       Impact factor: 1.880

3.  Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA.

Authors:  I Abe; G D Prestwich
Journal:  Proc Natl Acad Sci U S A       Date:  1995-09-26       Impact factor: 11.205

  3 in total

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