Isolation and Identification of a Sulfakinin-Like Peptide, with Sequence Homology to Vertebrate Gastrin and Cholecystokinin, from the Brain of Locusta Migratoria
A neuropeptide (pGlu-Leu-Ala-Ser-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-NH2) with a blocked N-terminus and related to leucosulfakinins I and II from the Madeira roach has been isolated from an extract of 9000 brain complexes of Locusta migratoria. The peptide stimulates the motility of the cockroach hindgut. Biological activity was monitored during purification by high performance liquid chromatography by observing the myotropic effect of column fractions on the isolated hindgut of Leucophaea moderne.
The peptide, designated as locustasulfakinin or Lom-SK shares a common C-terminal decapeptide fragment with leucosulfakinin II and a common heptapeptide fragment with leucosulfakinin I, indicating the importance of the constituent amino acids for biological activity. Locust asulfakinin is the third invertebrate neuropeptide which exhibits sequence homologies with the hormonally active fraction of the vertebrate hormones cholecystokinin, human gastrin II and caerulin. Its intestinal myotropic activity is analogous to that of gastrin and cholecystokinin. The sequence homologies as well as the analogous myotropic activities suggest that gastrin/cholecystokinin-like peptides have a long evolutionary history, and probably play an important role in physiology.
KeywordsHigh Performance liqUid Chromatography Single Base Substitution High Performance liqUid Chromatography Column High Performance liqUid Chromatography Condition Human Gastrin
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