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Six sulphated octapeptide amide analogues, representing the C-terminal sequence of pancreozymin have been prepared in addition to the natural sequence. The tryptophyl residue which is essential for biological activity was replaced in this series by structurally, closely related analogues each of which resemble the properties of the original moiety to varying extents. The syntheses were so conducted that the C-terminal tetrapeptide amides (modified tetragastrins) could be secured. The results of the measurement of one of the biological parameters are indicated. The activity was determined to elucidate which of the physicochemical properties of the tryptophyl residue is most essential for exertion of biological activity in the described test.
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
February 1979,
International journal of peptide and protein research,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
January 1976,
Scandinavian journal of gastroenterology,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
January 1989,
Polish journal of pharmacology and pharmacy,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
April 1981,
Gastroenterology,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
November 1975,
Nature,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
July 2014,
Organic letters,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
September 1993,
The American journal of physiology,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
November 1976,
Chemical & pharmaceutical bulletin,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
October 2000,
Journal of medicinal chemistry,
H M Rajh, and
E C Mariman, and
G I Tesser, and
R J Nivard
June 1974,
The American journal of roentgenology, radium therapy, and nuclear medicine,
