PROPERTIES OF PURIFIED SQUALENE-HOPENE CYCLASE FROM BACILLUS-ACIDOCALDARIUS

被引：51

作者：

OCHS, D

TAPPE, CH

GARTNER, P

KELLNER, R

PORALLA, K

机构：

[1] UNIV TUBINGEN,INST BOT,AUF MORGENSTELLE 1,W-7400 TUBINGEN 1,GERMANY

[2] UNIV TUBINGEN,INST ORGAN CHEM,W-7400 TUBINGEN 1,GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 194卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19429.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The squalene‐hopene cyclase from Bacillus acidocaldarius cytoplasmic membrane, was purified to homogeneity by solubilization with Triton X‐100, chromatography on DEAE‐cellulose, phenyl Sepharose and two gel‐filtration columns. The enzyme monomer had a molecular mass of 75 kDa. The sequence of the first 23 amino acids was determined by Edman degradation. The enzyme activity was efficiently inhibited by n‐alkyldimethylammonium halides with alkyl chain lengths between 12 and 18 C atoms. Inhibition was also observed with (5‐hydroxycarvacryl)trimethylammonium chloride 1‐piperidine carboxylate, dodecyldimethylamine N‐oxide, azasqualene and farnesol. Competitive inhibition with dodecyltrimethylammonium bromide, (5‐hydroxycarvacryl)trimethylammonium chloride 1‐piperidine carboxylate and dodecyldimethylamine N‐oxide was demonstrated by Lineweaver‐Burk plots. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：75 / 80

页数：6

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