Isolation of the Maclura pomifera hemagglutinin on a deoxymelibiotol affinity support and preliminary characterization by buffer electrofocusing and high-performance liquid chromatography.
Maclurin, the potent non-specific blood-group hemagglutinin present in extracts of Maclura pomifera, has been purified by a new biospecific affinity-chromatographic procedure. Additional studies have indicated that this hemagglutinin occurs as five closely related tetrameric protein isoforms derived from two non-covalently-linked polypeptide chains, mol. wts. ca. 10,000 and 13,000 respectively. Buffer electrofocusing fractionated the lectin into 12 components; the major isolectin exhibited an isoelectric point at pH 4.8.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D006384:Hemagglutination; D006801:Humans; D007525:Isoelectric Focusing; D037102:Lectins / Q000302:isolation & purification* / Q000494:pharmacology; D046911:Macromolecular Substances; D008553:Melibiose / Q000031:analogs & derivatives; D008970:Molecular Weight; D037121:Plant Lectins; D051381:Rats; D012639:Seeds / Q000032:analysis*; D012756:Sheep
D000596:Amino Acids; D037102:Lectins; D046911:Macromolecular Substances; D037121:Plant Lectins; C034551:maclurin; D008553:Melibiose