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Plant and Cell Physiology, 1994, Vol. 35, No. 8 1141-1147
© 1994

A Factor from Pea Cotyledons That Modifies Auxin-Induced {alpha}-Amylase in vitro

Eiji Hirasawa and Naoko Higashimoto1

Department of Biology, Faculty of Science, Osaka City University Sumiyoshi-ku, Osaka, 558 Japan

An auxin-induced {alpha}-amylase (AMY I; EC 3.2.1.1 [EC] ) 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.

1Present address: Shionogi & Co. Ltd., Fukushima-ku, Osaka, 553 Japan

(Received May 26, 1994; Accepted August 22, 1994)
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