Hydrokinetic activity of secretion and secretin analogues, modified in the N-terminal sequence, and of vasoactive intestinal peptide in the dog pancreas.

Abstract:

:In the dog pancreas in vivo, the biological activity of secretin and vasoactive intestinal peptide was compared to that of secretin analogues modified in their N-terminal hexapeptide and to X-secretion (alpha, beta-Asp3-secretin) and Y-secretin (a conversion product of X-secretin consisting of about 15% secretin and 85% beta-Asp3-secretin). Replacement of Asp3 by glutamic acid reduced secretin activity markedly. Replacement by neutral amino acids abolished the activity nearly completely. alpha, beta-Asp3-secretin and beta-Asp3-secretin appeared to be ineffective. The results indicate that the free beta-carboxy group of the side chain of the Asp3 residue of the secretin molecule is of decisive importance for hydrokinetic action.

journal_name

Digestion

journal_title

Digestion

authors

Lehnert P,Forell MM,Jaeger E,Moroder L,Wünsch E

doi

10.1159/000198600

subject

Has Abstract

pub_date

1981-01-01 00:00:00

pages

85-8

issue

2

eissn

0012-2823

issn

1421-9867

journal_volume

22

pub_type

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