FEBS Letters · 1991 · 63 citations · 19 references
Life SciencesBiochemistryMolecular BiologyImmunophysiologyImmunoregulationInflammationImmunoassay AnalysisPeptide AnalysisAntiserum PreparationProtein ToxinsReactivitySynthetic Peptide AntigensSynthetic Peptide CharacterizationToxin Antigenicity
Antisera were raised to a synthetic peptide which represents the predicted C-terminal decapeptide of the alpha subunit of the G-proteins Gq and G11. Competitive ELISA indicated that antiserum CQ2 displayed strong reactivity against this peptide. Antiserum CQ2 identified an apparently single polypeptide of 42 kDa which was expressed widely. The mobility of this polypeptide in SDS-PAGE was not modified by pretreatment of cells with pertussis toxin, indicating that it was not a substrate for this toxin. Furthermore, the levels and mobility of this polypeptide were unaltered by treatment of cells with cholera toxin, defining that it was not related to Gs alpha.
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William F. Simonds, Paul K. Goldsmith, Juan Codina et al. · Proceedings of the National Academy of Sciences · 1989 · 375 citations · Full text