Isolation of three types of Gi from bovine spleen

Biochemical and Biophysical Research Communications
R MorishitaT Asano

Abstract

We have previously reported the purification of two alpha subunits of G proteins, Gi2 and Gi3, from bovine spleen. However, it recently became clear that the preparation of Gi3 alpha contained a significant amount of Gi1 alpha by the immunoblot analysis using specific antibodies. In this study, we purified these G proteins as a trimer form from bovine spleen, and obtained following results. (1) Gi3 was separated from Gi1 using Mono Q column chromatography. Isoelectric focusing was employed to distinguish Gi3 from Gi1 in the column eluates. (2) Purified Gi2 and Gi3 retained much higher activities to bind GTP gamma S or to be ADP-ribosylated by pertussis toxin than the alpha subunits purified previously. (3) Using these spleen Gi2 and Gi3 and bovine brain Gi1, the parameter of GTP gamma S binding to the three types of Gi was compared. Three Gis showed different rates of GTP gamma S binding but showed the similar Kd values.

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Jun 30, 1989·Biochemical and Biophysical Research Communications·R MorishitaY Kaziro
May 12, 1988·Nature·E J Neer, D E Clapham
Jun 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S Y KimE J Neer
Dec 1, 1973·Analytical Biochemistry·W Schaffner, C Weissmann

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