Isolation of an arabinogalactan protein by lectin affinity chromatography on tridacnin-Sepharose 4B

Abstract

An arabinogalactan protein from the style canal of Gladiolus has been isolated by a one-step procedure involving lectin affinity chromatography, using the galactose-binding lectin from the small giant clam, Tridacna maxima, coupled to Sepharose 4B. The lectin binding is calcium-ion dependent, so that the arabinogalactan protein which is bound to the column in the presence of calcium can be eluted by washing the column with a calcium-free buffer. This method has a general utility for the purification of polysaccharides and glycoproteins containing β-linked galactosyl residues. © 1979.