Abstract
Melittin mRNA from queen bee venom glands was translated in a cell-free system from wheat germ. A product larger than promelittin was formed which had the carboxy-terminal sequence -Gln-Gln-GlyCOOH. Melittin and promelittin from venom glands terminated in -Gln-GlnCONH2. The possible role of the extra glycine residue in the formation of a COOH-terminal amide via a transamidase-like reaction was discussed.