Purification of GTP-binding proteins from bovine brain membranes. Identification of heterogeneity of the alpha-subunit of Go proteins

FEBS Letters
I KobayashiT Katada

Abstract

Using high-resolution Mono Q column chromatography, we purified 6 distinct peaks of GTP-binding proteins from bovine brain membranes. Five of them consisted of 3 polypeptides with alpha beta gamma-subunits and served as the substrate of islet-activating protein (IAP), pertussis toxin. The other one was purified as alpha-subunit alone and was also ADP-ribosylated by IAP in the presence of beta gamma-subunits. When each alpha-subunit was characterized by immunoblot analysis using various antibodies with defined specificity, the two of them were identified as Gi-1 and Gi-2, and other 4 appeared to be Go or Go-like G proteins. The alpha-subunits of immunologically Go-like proteins were apparently distinguishable from one another on elution profiles from the Mono Q column. Thus, there was a heterogeneity of the alpha-subunit of Go in the brain membranes.

References

Jun 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·H ItohK Suzuki
Dec 1, 1973·Analytical Biochemistry·W Schaffner, C Weissmann

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Citations

Feb 13, 2009·Neuro-Signals·Meisheng Jiang, Neil S Bajpayee
Feb 17, 1999·Proceedings of the National Academy of Sciences of the United States of America·T ExnerB Nürnberg
Jul 1, 1991·Journal of Neurochemistry·J N LaroccaR W Ledeen
Aug 3, 2002·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Peter AdamsonJohn Greenwood
Mar 3, 1995·The Journal of Biological Chemistry·M D WilcoxJ D Hildebrandt
May 1, 1992·Archives of Biochemistry and Biophysics·K KontaniT Katada
Mar 1, 1991·Kidney International·R T Miller

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