Abstract
The hydrodynamic properties of the G i2 α-subunit in human neutrophil cytosol were analyzed. The s 20,w value was 3.3 S at 30°C and 4.1 S at 4°C. Reconstitution of the cytosolic α-subunit with βγ-complex purified from porcine brain resulted in an s 20,w value of 4.0 S at 30°C and 4.2 S at 4°C. Treatment of cytosol with G-protein-activating agents, GTPγS and MgCl 2, decreased the s 20,w value to 2.4 S at 30°C and 2.9 S at 4°C. Our results indicate that the cytosolic α-subunit of neutrophils is an inactive monomeric species at 30°C capable of interacting with G-protein βγ-complex and responsive to treatment with activating agents leading to the two activated forms, α* at 4°C and α** at 30°C.
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