A Factor from Pea Cotyledons That Modifies Auxin-Induced α-Amylase in vitro : PROTEINS, ENZYMES AND METABOLISM
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概要
- 論文の詳細を見る
An auxin-induced α-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 α-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.
- 日本植物生理学会の論文
著者
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Hirasawa Eiji
Department Of Agricultural Chemistry Kyoto University
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Higashimoto Naoko
Department of Biology, Faculty of Science, Osaka City University
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