Peer-reviewed veterinary case report
Receptor binding of guinea pig and pig vasoactive intestinal peptides by rat lung
- Journal:
- Biochemical Journal
- Year:
- 1988
- Authors:
- Paul, S et al.
- Affiliation:
- Department of Pharmacology, University of Nebraska Medical Center, Omaha, NE 68105, U.S.A. · United States
- Species:
- rodent
Abstract
Guinea pig vasoactive intestinal peptide (gpVIP) differs from other mammalian VIPs in four of its 28 amino acid residues. In the present study, the gpVIP displaced 125I-labelled pig VIP (pVIP) binding by rat lung membranes with 7.7-fold lower potency than pVIP. Degradation of gpVIP by rat lung membranes, assessed by radioimmunoassay and h.p.l.c., was 1.9-fold greater than that of pVIP. This difference in degradation of the two peptides was not large enough to account for the lower receptor-binding potency of gpVIP. The amino acid residues that distinguish pVIP from gpVIP are likely to contribute to the interaction of VIP with receptors and peptide hydrolases in lung membranes.
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Search related cases →Original publication: https://doi.org/10.1042/bj2540613