Isolation of theMaclura pomiferahemagglutinin on a deoxymelibiotol affinity support and preliminary characerization by buffer electrofocusing and high-performance liquid chromatography

Abstract
Maclurin, the potent nonspecific blood-group hemagglutinin present in extracts of M. pomifera, was purified by a new biospecific affinity-chromatographic procedure. This hemagglutinin apparently occurs as 5 closely related tetrameric protein isoforms derived from 2 non-covalently-linked polypeptide chains, MW .apprx. 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.