Isolation, structure and properties of the C-terminal flanking peptide of preprocholecystokinin from rat brain.
The C-terminal flanking peptide of preprocholecystokinin has been isolated from rat brain. Micro-sequence analysis revealed the primary structure: Ser-Ala-Glu-Asp-Tyr-Glu-Tyr-Pro-Ser. Arylsulphatase and mild acid hydrolysis suggested that both tyrosine residues are sulphated. The peptide was not active in bioassay systems that respond to CCK8; the significance of the conserved tripeptide Ser-Ala-Glu is discussed.
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002766:Cholecystokinin / Q000032:analysis*; D006168:Guinea Pigs; D009119:Muscle Contraction / Q000187:drug effects; D010446:Peptide Fragments / Q000302:isolation & purification* / Q000494:pharmacology; D011498:Protein Precursors / Q000032:analysis*; D011863:Radioimmunoassay; D051381:Rats; D012844:Sincalide / Q000494:pharmacology
D010446:Peptide Fragments; D011498:Protein Precursors; C042082:preprocholecystokinin; D002766:Cholecystokinin; D012844:Sincalide