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. 1990 Jun 15;169(2):816-23.
doi: 10.1016/0006-291x(90)90404-b.

Purification and characterization of a novel GTP-binding protein with a Mr value of 24,000 from rat liver

T Ohmori  1 , Y Takeyama, T Ueda, M Hiroyoshi, H Nakanishi, H Ohyanagi, Y Saitoh, Y Takai
Affiliations

Purification and characterization of a novel GTP-binding protein with a Mr value of 24,000 from rat liver

T Ohmori et al. Biochem Biophys Res Commun. .

Abstract

About 15% of the total GTP-binding proteins (G proteins) of rat liver homogenate was found in the microsomes-Golgi complex fraction. From this fraction, we purified to near homogeneity and characterized a G protein with a Mr value of 24,000 (24K G). 24K G specifically bound guanosine 5'-(3-Q-thio) triphosphate (GTP gamma S), GTP and GDP with a Kd value for GTP gamma S of about 30 nM. 24K G bound maximally about 0.7 mol of GTP gamma S/mol of protein. 24K G hydrolyzed GTP to liberate Pi with a turnover number of about 0.008 min-1. 24K G was not copurified with the beta gamma subunit of heterotrimeric G proteins. The partial amino acid sequences of 24K G revealed that this protein was a novel small G protein.

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