MULTIPLE FORMS OF THE CONSTITUTIVE WHEAT CINNAMYL ALCOHOL-DEHYDROGENASE

被引：30

作者：

PILLONEL, C ^{[1
]}

HUNZIKER, P ^{[1
]}

BINDER, A ^{[1
]}

机构：

[1] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

来源：

JOURNAL OF EXPERIMENTAL BOTANY | 1992年 / 43卷 / 248期

关键词：

CINNAMYL ALCOHOL DEHYDROGENASE; LIGNIN; TRITICUM-AESTIVUM L;

D O I：

10.1093/jxb/43.3.299

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Three cinnamyl alcohol dehydrogenase (CAD) isoenzymes were separated from etiolated wheat seedlings (Triticum aestivum L.) and examined by native gel electrophoresis. Two of these enzymes (CAD-1 and CAD-2) were purified to apparent homogeneity. They exhibited a marked difference in substrate affinity. On sodium dodecyl sulphate-acrylamide gel the isolated isoenzymes showed only one protein band each with an M(r) 45 000 and 40 000 daltons, respectively, whereas on native gel two bands were identified for each protein. Isoenzymes from a variety of diploid, tetraploid. and hexaploid wheats were compared. The results indicated that the CAD polymorphism could be genetically determined.

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页码：299 / 305

页数：7

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