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
Digestionjournal_title
Digestionauthors
Lehnert P,Forell MM,Jaeger E,Moroder L,Wünsch Edoi
10.1159/000198600subject
Has Abstractpub_date
1981-01-01 00:00:00pages
85-8issue
2eissn
0012-2823issn
1421-9867journal_volume
22pub_type
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