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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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

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

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References (40)

Publisher
Springer Journals
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
DOI
10.1023/A:1005807010811
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 29, 2004

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