Purification and characterization of a galactoside-binding lectin from human brain

A beta-galactoside-binding hemagglutinin was detected in soluble extracts of human brain. This soluble lectin was purified to homogeneity by affinity column chromatography on lactose coupled to divinylsulfone-activated agarose. The purified lectin had an isoelectric point of 3.9 and its subunit molecular mass estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate was 14,500. Human brain lectin was not a glycoprotein and its amino acid composition was characterized by a high content of serine, glutamic acid, and glycine, and a low content of methionine and cysteine. The most potent saccharide inhibitors tested were thiodigalactoside, lactose, and p-nitrophenyl-beta-D-galactoside. An antibody was raised to the pure lectin. Immunological relationships were found between the brain lectin and several other soluble lectins of various vertebrate origins.