Other

Kabigen Ab

Skandigen Ab

Kabigen Ab and Skandigen Ab

Viktor Mutt

Hans Jornvall

Hans G Boman

Sami I Said

Jong-Youn Lee

Mats Carlquist

Wolf-Georg Forssmann

Mats Andersson

Guro Gafvelin

Catja Johansson

Lars Thulin

Ann Nilsson

78 residue polypeptide (NK-lysine) and its use

Polypeptides and their use

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.

Antibacterial polypeptides

Mammal intestinal hormone precursor and its use

Human intestinal hormone and its use

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.

Vasoactive lung polypeptides

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.

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.

Vasoactive intestinal peptide from fowl

Growing community of inventors

Solua, Sweden

Viktor Mutt