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Conlon, J.M. et al.

Conlon, Warner, Burcher,

Bufokinin: a substance P-related peptide from the gut of the toad, Bufo marinus with high binding affinity but low selectivity for mammalian tachykinin receptors.

A tachykinin peptide, termed bufokinin, was isolated in pure form from an extract of the intestine of the toad, Bufo marinus, and its primary structure was established as: Lys-Pro-Arg-Pro-Asp-Gln-Phe-Tyr-Gly-Leu-Met.NH2. This sequence was confirmed by chemical synthesis and shows four amino acid substitutions (Arg1 --> Lys,Lys3 --> Arg,Gln5 --> Asp and Phe8 --> Tyr) compared with substance P. Binding parameters for synthetic bufokinin and mammalian tachykinins were compared using receptor-selective radioligands and crude membranes from rat tissues enriched in the NK-1 (submandibular gland) , NK-2 (stomach fundus) and NK-3 (brain) receptors. In terms of inhibiting the binding of the selective radioligands, bufokinin (Kd = 0.3 nM) was 1.8-fold more potent than substance P at the rat NK-1 site, but it was only 2-fold less potent (Kd = 2.8 nM) than neurokinin A at the NK-2 site and only 2-fold less potent (Kd = 48 nM) than neurokinin B at the NK-3 site. Thus, bufokinin shows relatively high affinity but lack of selectivity for all three tachykinin binding sites in rat tissues.[1]

References

Bufokinin: a substance P-related peptide from the gut of the toad, Bufo marinus with high binding affinity but low selectivity for mammalian tachykinin receptors. Conlon, J.M., Warner, F.J., Burcher, E. J. Pept. Res. (1998) [Pubmed]

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