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- W133900510 abstract "The naturally occurring bombesin (Bn)-related peptides can be divided structurally into three different groups based on chemical structure (Erspamer 1988; Erspamer and Melchiorri 1977; Minamino et al. 1983, 1984). The amphibian peptide Bn resembles other amphibian peptides such as alytesin and the mammalian peptide gastrin-releasing peptide (GRP) (Anastasia et al. 1971; Erspamer 1988; Erspamer and Melchiorri 1977; McDonald et al. 1979) in possessing a carboxy terminal Gly-His-Leu-Met-amide (Fig. 1). The second class includes the amphibian peptides ranatensin and litorin, which resemble the mammalian peptide neuromedin B (Erspamer 1988; Erspamer and Melchiorri 1977; Minamino et al. 1983, 1984) in possessing a COOH terminal Gly-His-Phe-Met-amide (Table 1). The third group, comprised of the amphibian peptide phyllolitorin and other structurally related amphibian peptides, have at present no mammalian counterpart and are characterized by having a COOH terminal Gly-Ser-Phe-Met-amide or Gly-Ser-Leu-Met-amide (Erspamer 1988) (Table 1)." @default.
- W133900510 created "2016-06-24" @default.
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- W133900510 date "1993-01-01" @default.
- W133900510 modified "2023-09-25" @default.
- W133900510 title "Bombesin Receptor Antagonists: Different Classes and Cellular Basis of Action" @default.
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- W133900510 doi "https://doi.org/10.1007/978-3-642-84956-5_8" @default.
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