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J. Biol. Chem., Vol. 263, Issue 14, 6476-6479, 05, 1988
P Goldsmith, K Rossiter, A Carter, W Simonds, CG Unson, R Vinitsky and AM Spiegel
Three closely related, but distinct, GTP-binding proteins (G-proteins) are
encoded by cDNAs arbitrarily designated Gi1, Gi2, and Gi3. The in vitro
translated products of mRNAs prepared from Gi1, Gi2, and Gi3 cDNAs migrate
as 41-, 40-, and 41-kDa proteins, respectively, on sodium dodecyl
sulfate-polyacrylamide gels. Antisera were raised against synthetic
decapeptides corresponding to a divergent sequence (residues 159-168 for
Gi1 and Gi3; 160-169 for Gi2) of the three cDNAs and tested on immunoblots
for reactivity with three purified G-proteins, G41 and G40 from brain and
G41 from HL-60 cells. LD antisera (Gi1 peptide) react only with brain G41.
LE antisera (Gi2 peptide) react only with brain G40, and SQ antisera (Gi3
peptide) react exclusively with HL-60 G41. The results indicate that the
41-kDa G-protein purified from HL-60 cells differs from the purified brain
41-kDa protein and suggest that the HL-60 cell protein corresponds to that
encoded by Gi3 cDNA.
Identification of the GTP-binding protein encoded by Gi3 complementary DNA
Metabolic Diseases Branch, National Institute of Diabetes, Digestive, and Kidney Diseases, Bethesda, Maryland 20892.
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