Primary structure and synthesis of a blocked myotropic neuropeptide isolated from the cockroach, Leucophaea maderae.
A peptide which stimulates the contractile activity of the cockroach hindgut was isolated from head extracts of the cockroach, Leucophaea maderae. The inability of aminopeptidase M to degrade the peptide and the presence of glutamic acid in the hydrolysate suggested N-terminal blocking by pyroglutamic acid. The N-terminal pGlu was removed enzymatically and the unblocked fragment was sequenced with an automated gas-phase peptide sequencer. The structure determined (pGlu-Thr-Ser-Phe-Thr-Pro-Arg-Leu-NH2) was synthesized and shown to be both chemically and biologically identical with the natural product.
D000595:Amino Acid Sequence; D000818:Animals; D003058:Cockroaches / Q000378:metabolism*; D004064:Digestive System / Q000187:drug effects; D009119:Muscle Contraction / Q000187:drug effects; D009479:Neuropeptides / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology
D009479:Neuropeptides