Characterization of the putative α subunit of a heterotrimeric G protein in rice

被引:3
作者
Yukimoto Iwasaki
Teruhisa Kato
Toshio Kaidoh
Atsushi Ishikawa
Tadashi Asahi
机构
[1] Fukui Prefectual University,Department of Bioscience, Faculty of Biotechnology
来源
Plant Molecular Biology | 1997年 / 34卷
关键词
ADP ribosylation; α subunit; cholera toxin; heterotrimeric G protein; rice; signal transduction;
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中图分类号
学科分类号
摘要
A recombinant protein with a cDNA that encodes the putative α subunit of a rice heterotrimeric G protein was synthesized in Escherichia coli and purified. The recombinant protein (rGrice α) with an apparent molecular mass of 45 kDa was bound with guanosine 5′-(3-O-thio)triphosphate with an apparent association constant (kapp) of 0.36. The protein also hydrolyzed GTP and its Kcat was 0.44. rGrice α was ADP-ribosylated by activated cholera toxin.
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页码:563 / 572
页数:9
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