Abstract
The influence of the position of the sulphate group in CCK on its gastric acid and pepsin stimulating activities was investigated in conscious cats with gastric fistulae. In Boc-CCK7, substitution of tyrosine-SO 3H by ϵ-hydroxynorleucine-SO 3H, an aliphatic amino acid approximating the length of tyrosine, enhanced acid secretory potency, whilst similar substitution by serine-SO 3H reduced potency, possibly due to the serine residue holding the sulphate group closer to the peptide backbone. Desulphation of Ser-CCK6 reduced acid secretory potency indicating that the known loss of potency upon desulphation of CCK-like peptides is not wholly dependent upon the presence of tyrosine residue in position 7. Sulphated CCK-like peptides are partial agonists of pepsin secretion, and desulphation confers full agonist activity. Analogues of CCK with serine or ϵ-hydroxynorleucine substituting for tyrosine, whether sulphated or not, showed full agonist activity in stimulating pepsin secretion. These data suggest the presence of the aromatic tyrosine residue, as well as sulphation, to be a necessary prerequisite for pepsin partial agonist activity in CCK-like peptides.
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