Polyclonal antibodies directed against the two components of EF-1, the
G-protein EF-1 alpha and the guanine-nucleotide exchange complex EF-1
beta gamma delta, were used for the analysis of EF-1. We show that Xe
nopus oocytes as well as Xenopus A6 cultured cells contain comparable
ratios around 2:1 of EF-1 alpha versus EF-1 beta gamma delta. Immunolo
calization of EF-1 was analyzed in A6 cultured cells. Both components
appeared to be mainly localized in the cytoplasmic compartment, as a g
ranulous diffuse network forming a gradient from the nucleus to the pe
riphery of the cells. The major fraction of EF-1 was correlated to end
oplasmic reticulum localization and not to the microtubule network. Co
-localization of EF-1 with the endoplasmic reticulum is consistent wit
h the function of EF-1 in peptide chain elongation.