title: Purification of a peptide with venoconstrictor and vasodepressor activity, from Cohn fraction III-O of human plasma protein.
abstract: Cohn fraction III-O of human plasma proteins has previously been shown to contain a peptide which produces vasodilator responses in intact vascular beds. This peptide has bradykinin-like pharmacological actions but it can be distinguished from bradykinin. A process of serial fractionation of Cohn fraction III-O on Sephadex CM-25 and G-25 gels, followed by ion exchange chromatography with gradient elution on a Bio-Rex 70 column and subsequent desalting has permitted purification of this peptide. Amino acid analysis suggested a peptide with 14 amino acyl-residues and a calculated molecular weight of 1,780. The purified material retained the vasodilator properties of impure sources of the peptide, but was highly unstable. There was no interaction with anti-bradykinin antibodies.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001798:Blood Proteins / Q000032:analysis / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006801:Humans; D008970:Molecular Weight; D014665:Vasodilator Agents / Q000032:analysis / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D001798:Blood Proteins; D014665:Vasodilator Agents