Abstract
Abstract Elongation factor 2 (EF-2) and ADP ribosylated EF-2 appear to have the same amino acid composition and to consist of one polypeptide chain of approximately 1,000 residues with valine as the NH2-terminal residue; the molecular weight calculated from the composition is 110,000 per mole of either protein or adenosine-5'-diphosphate-5'-ribose (ADPR). Titration with p-hydroxymercuri[14C]benzoate indicated 18 sulfhydryls and 2 disulfides per mole of EF-2. EF-2 could not be ADP ribosylated if first titrated with p-hydroxymercuribenzoate. Titration of EF-2 and ADPR EF-2 was compared as well as titration of EF-2 ± GTP and ± diphtheria toxin fragment A; certain differences were observed.
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