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Preliminary study of brassinosterone binding sites from mung bean epicotyls

Xu Rujuan, He Yujiong, Wang Yuqin, Zhao Yuju

Shanghai Institute of Plant Physiology, Chinese Academy of Sciences. Shanghai

Abstract

Different fractions of mung bean epicotyl extract were tested for brassinosterone binding. The 10 000×g fraction showed stronger brassinosterone binding than other fractions (Table 1). The brassinosterone binding to 10 000×g fraction was saturated after a 1 h incubation (Fig.1). The binding was temperature-dependent, showing a maximum at 4℃ (Fig.2). The amount of brassinosterone bound is dependent on pH, the optimal pH being 7.5(Fig.3). Trypsin treatment weakened the brassinosterone binding (Fig.4). This result indicates that proteins may be involved in the brassinosterone-binding site. Several analogues of brassinosterone could also bind to the brassinosterone-binding site to various extents(Table 2).

Key words: Brassinosterone;Mung bean;Epicotyl;Binding site

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Citing This Article：

Xu Rujuan, He Yujiong, Wang Yuqin, Zhao Yuju. Preliminary study of brassinosterone binding sites from mung bean epicotyls. Acta Physiol Sin 1994; 46 (3): (in Chinese with English abstract).