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Biomedical subjects

V Mutt

Publications and source records attributed to V Mutt.

At least 199 records · Page 11Linked to original sources
PubMed1970

Further purification of a polypeptide demonstrating enterogastrone activity.

1. The further purification of a polypeptide having potent enterogastrone activity, without CCK-PZ effects, is described.2. The material was inhibitory when doses of 1.0 mug/kg.hr were administered intravenously. Amino acid analyses demonstrated the absence of proline, a high content of glutamine and a preponderance of lysine over arginine. Tryptic degradation destroys the inhibitory effect of the polypeptide. Further studies must be performed before the physiological status of the polypeptide can be ascertained.

Alginates↗
PubMedDate not supplied

Effect of porcine gastrin releasing peptide on gastric secretion and motility and the release of hormonal peptides in conscious cats.

The effect of porcine gastrin releasing peptide (GRP) was compared to those of bombesin (BBS) and pentagastrin (PG) in conscious cats. GRP and BBS augmented acid and pepsin secretions, as well as antral motility with an early effect comparable to that produced by pentagastrin with an elevation of low amplitude contractions and a diminution of high amplitude contractions. BBS and GRP increased plasma gastrin and pancreatic polypeptide (PP) levels and decreased motilin levels measured by a C terminus-directed antiserum. In all cases, BBS and GRP displayed parallel dose-response curves. PG showed slight differences in the slopes of the dose-response curves slopes of the dose-response curves except for acid secretion stimulation where no difference was noted (PG was the most effective) and for pepsin stimulation where the difference was large (PG was much less effective). According to the different targets studied, BBS was 4 to 9 times more potent than GRP, 6 to 200 times more than PG. Gastrin release, elicited by the lowest ED50 of both BBS and GRP, should be considered as their primary effect in the cat.

Animals↗
PubMedDate not supplied

Isolation and characterization of a variant form of vasoactive intestinal polypeptide.

A variant form of the vasoactive intestinal polypeptide (VIP) has been isolated. It was found to consist of a molecule which instead of the C-terminal asparagine amide of VIP has a C-terminal extension of Gly-Lys-Arg. This VIP variant displaces VIP in a VIP receptor assay, reacts with N-terminally-directed antisera in a VIP radioimmunoassay and possesses VIP-like bioactivity in an assay measuring pancreatic juice secretion in the cat.

Amino Acids↗