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J. Biol. Chem., Vol. 261, Issue 2, 631-637, 01, 1986
PC Sternweis
The purified G-proteins from bovine brain were examined for potential
solubility in the absence of detergent. The isolated alpha o and alpha i
subunits migrated through sucrose with rates consistent with the existence
of monomeric species either in the presence or the absence of cholate. The
beta gamma subunits or holo-G-proteins aggregated extensively if cholate
was absent. Al3+, Mg2+, and F- prevented the aggregation of alpha o and
alpha i caused by the addition of beta gamma and could also prevent the
aggregation of alpha s when Gs was examined at higher temperature. The
association of subunits with phospholipid vesicles was examined. Whereas
beta gamma associated totally with phospholipid vesicles, purified alpha o
showed little interaction. alpha o did bind to vesicles containing beta
gamma (beta gamma vesicles) in a saturable fashion that indicated a
stoichiometric association between the subunits. Treatment with guanosine
5'-(3-O- thio)triphosphate could partially dissociate alpha o that was
bound to beta gamma vesicles. These data suggest that beta gamma may be an
anchor for association of alpha subunits with membranes and that regulation
by these proteins may not be limited to the plasma membrane. This
possibility and its implications are discussed. The reversible association
of alpha o to beta gamma vesicles may provide a very sensitive system for
the study of the interactions between these subunits.
The purified alpha subunits of Go and Gi from bovine brain require beta gamma for association with phospholipid vesicles
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