Purification of geranylgeranyl diphosphate synthase from Sinapis alba etioplasts
作者： André Laferrière , Peter Beyer
DOI: 10.1016/0167-4838(91)90054-4
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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 column, competitive inhibitor aminophenylethyl linked spacer arm matrix via amino group. The native protein apparently formed homodimers with molecular mass monomer 38 kDa. antibodies raised against enzyme were inhibitory prenyl-forming activities homologous system as well stroma fraction dalfodil (Narcissus pseudonarcissus L.) chromoplasts.
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