PURIFICATION OF GERANYLGERANYL DIPHOSPHATE SYNTHASE FROM SINAPIS-ALBA ETIOPLASTS

被引：33

作者：

LAFERRIERE, A ^{[1
]}

BEYER, P ^{[1
]}

机构：

[1] UNIV FREIBURG,INST BIOL 2,SCHANZLESTR 1,W-7800 FREIBURG,GERMANY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1991年 / 1077卷 / 02期

关键词：

GERANYLGERANYL DIPHOSPHATE SYNTHASE; ENZYME PURIFICATION;

D O I：

10.1016/0167-4838(91)90054-4

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：

Geranylgeranyl diphosphate synthase was purified to homogeneity from mustard (Sinapis alba) etioplasts in a two-step procedure employing FPLC ion-exchange chromatography and an affinity column. For the construction of the affinity column, the competitive inhibitor aminophenylethyl diphosphate was linked to the spacer arm of the matrix via the amino group. The native protein apparently formed homodimers with a molecular mass of the monomer of 38 kDa. The antibodies raised against the purified enzyme were inhibitory to prenyl-forming enzyme activities in the homologous system as well as in a stroma fraction from daffodil (Narcissus pseudonarcissus L.) chromoplasts.

引用

页码：167 / 172

页数：6

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