A FACTOR FROM PEA COTYLEDONS THAT MODIFIES AUXIN-INDUCED ALPHA-AMYLASE IN-VITRO

被引：0

作者：

HIRASAWA, E

HIGASHIMOTO, N

机构：

[1] Department of Biology, Faculty of Science, Osaka City University, Sumiyoshi-ku, Osaka

来源：

PLANT AND CELL PHYSIOLOGY | 1994年 / 35卷 / 08期

关键词：

AFFINITY FOR STARCH; AUXIN-INDUCED ALPHA-AMYLASE (EC 3.2.1.1); COTYLEDON; MODIFICATION OF ALPHA-AMYLASE; PISUM SATIVUM;

D O I：

10.1093/oxfordjournals.pcp.a078707

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

An auxin-induced a-amylase (AMY I; EC 3.2.1.1) with a low affinity for potato starch was purified to homogeneity from detached cotyledons of Pisum sativum, as judged by the presence of a single band after non-denaturing PAGE and SDS-PAGE. AMY I was compared with a previously purified auxin-induced alpha-amylase (AMY II) that had a higher affinity for potato starch. No difference between AMY I and AMY II was apparent after SDS-PAGE or isoelectric focusing (IEF) and rates of degradation of soluble starch were identical. However, AMY I was less active than AMY II in the degradation of starch granules. A factor that converted AMY II to AMY I in vitro was detected in a crude extract of detached cotyledons. The factor was heat-labile.

引用

页码：1141 / 1147

页数：7

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