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

Characterization of the putative α subunit of a heterotrimeric G protein in rice 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. Plant Molecular Biology Springer Journals

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

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Kluwer Academic Publishers
Copyright © 1997 by Kluwer Academic Publishers
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
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