Conlon JM, Mechkarska M.

	Figure 1. Primary structures of the magainin peptides isolated from skin secretions of frogs belonging to the genera Xenopus and Silurana. The amino acid sequence of magainin-ST1 was deduced from the corresponding nucleotide sequence of genomic DNA. In order to maximize structural similarity, gaps denoted by * have been introduced into some sequences. Strongly conserved residues are shaded.
	Figure 2. Primary structures of the peptide glycine-leucine-amide (PGLa) peptides isolated from skin secretions of frogs belonging to the genera Xenopus and Silurana. a denotes C-terminal α-amidation. In order to maximize structural similarity, gaps denoted by * have been introduced into some sequences. Strongly conserved residues are shaded.
	Figure 3. Primary structures of the caerulein precursor fragment (CPF) peptides isolated from skin secretions of frogs belonging to the genera Xenopus and Silurana. a denotes C-terminal α-amidation. In order to maximize structural similarity, gaps denoted by * have been introduced into some sequences. Strongly conserved residues are shaded.
	Figure 4. Primary structures of the xenopsin precursor fragment (XPF) peptides isolated from skin secretions of frogs belonging to the genera Xenopus and Silurana. In order to maximize structural similarity, gaps denoted by * have been introduced into some sequences. Strongly conserved residues are shaded.
	Figure 5. Primary structures of the hymenochirins isolated from skin secretions of the frogs Hymenochirus boettgeri and Pseudhymenochirus merlini, and the pseudhymenochirins from P. merlini. a denotes C-terminal α-amidation. Strongly conserved residues are shaded.

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