Abstract: A 78 residue polypeptide comprising the following amino acid sequenceGYFCESCRKIIQKLEDMVGPQPNEDTVTQAASQVCDKLKILRGLCKKIMRSFLRRISWDILTGKK PQAICVDIKICKE [SEQ ID NO:1]:and functional derivatives and pharmaceutically acceptable salts thereof, said sequence comprising intra-linked half-cysteines; pharmaceutical composition containing such polypeptide as an active ingredient; a method for inhibiting microbial growth and cancer cell growth in animals including man; and nucleotide sequence corresponding to such polypeptide.

Abstract: Polypeptides comprising the following amino acid sequence: Arg-Arg-Arg-Pro-Arg-Pro-Pro-Tyr-Leu-Pro-Arg-Pro-Arg-Pro-Pro-Pro-Phe-Phe-Pr o-Pro-Arg-Leu-Pro-Pro-Arg-Ile-Pro-Pro-Gly-Phe-Pro-Pro-Arg-Phe-Pro-Pro-Arg-P he-Pro; pharmaceutical compositions containing such polypeptides; and a method of inhibiting bacterial growth using such polypeptides.

Abstract: A polypeptide having bactericidal activity, particularly against gram-negative bacteria, has been isolated from pig intestine. The porcine cecropin has the amino acid sequence: H.sub.2 N-Ser-Trp-Leu-Ser-Lys-Thr-Ala-Lys-Lys-Leu-Glu-Asn-Ser-AlaLys-Lys-Arg-Ile-S er-Glu-Gly-Ile-Ala-Ile-Ala-Ile-Gln-Gly-Gly-Pro-Arg-COOh. Pharmaceutical compositions containing such poypeptides, or functional derivatives thereof, are useful in therapeutic and prophylactic methods for inhibiting bacterial growth.

Abstract: A mammal intestinal hormone precursor having the following peptide structure: His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg-L-M-Ala-Arg-Leu-Gl n -Arg-Leu-Leu-Gln-Gly-Leu-Val-Gly-N-O, wherein L is Glu or Asp, M is Gly or Ser, and N and O are selected from Lys and Arg; compositions containing such precursor and a method of stimulating pancreatic secretion.

Abstract: A human intestinal hormone having the following peptide structure: His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg-Glu-Gly-Ala-Arg-Le u-Gln-Arg-Leu-Gln-Gly-Leu-Val-NH.sub. 2 ; compositions containing such hormone; and a method of stimulating pancreatic secretion.

Abstract: Vasoactive polypeptide fractions having biological activity isolated in purified form from animal lungs induce peripheral vasodilation and systemic hypotension. One of the peptides exhibits the property of relaxing isolated non-vascular smooth muscle organs while the other peptide contracted these tissues. The peptide fractions are obtained from the lungs of animals by procedures invloving boiling and mincing the lung, extracting the peptides into acetic acid, adsorbing by alginic acid, eluting with HCl and salting out, extracting into alchol, again adsorbed with alginic acid, fractionating by gel chromatography, e.g. on Sephadex G-25, and by ion exchange chromatography, e.g. on carboxymethyl cellulose, followed by further ion exchange chromatography and, optionally, countercurrent distribution.

Abstract: Vasoactive polypeptide fractions having biological activity isolated in purified form from animal lungs induce peripheral vasodilation and systemic hypotension. One of the peptides exhibits the property of relaxing isolated non-vascular smooth muscle organs while the other peptide contracted these tissues. The peptide fractions are obtained from the lungs of animals by procedures involving boiling and mincing the lung, extracting the peptides into acetic acid, adsorbing by alginic acid, eluting with HCl and salting out, extracting into alcohol, again adsorbed with alginic acid, fractionating by gel chromatography, e.g. on Sephadex G-25, and by ion exchange chromatography, e.g. on carboxymethyl cellulose, followed by further ion exchange chromatography and, optionally, countercurrent distribution.

Abstract: A polypeptide having important biological activity including systemic vasodilation, hypotension, increased cardiac output and bronchodilation is isolated from intestines of chickens. The isolation procedure for purification includes extraction, ion-exchange chromatography, gel chromatography and countercurrent distribution separation. The polypeptide has the general amino acid structure:His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Ser-Arg-Phe-Arg-Lys-Gln-Met-Ala-Val -Lys-Lys-Tyr-Leu-Asn-Ser-Val-Leu-Thr-NH.sub.2. Therapeutic biological actions may be produced in animals and humans by administration of 0.02-10 .mu.g of the peptide per kg of body weight.