Purification of Bacterial Neuraminidase (Receptor-destroying Enzyme)

Abstract

NEURAMINIDASE is the name now given to an enzyme the action of which is the hydrolytic cleavage of the glycosidic bond joining the keto group of N-acetylneuraminic acid to D-galactose or D-galactosamine¹. The enzyme was discovered in 1946 when Burnet, McCrea and Stone² found that filtrates of V. cholerae rendered human cells inagglutinable by influenza viruses. The factor responsible for this action was called the receptor-destroying enzyme by Burnet and Stone, who obtained some purification of the enzyme present in V. cholerae (strain 4 Z) filtrates by adsorption to and elution from red cells³. This technique was later incorporated into a three-step procedure for the partial purification of the enzyme⁴. Crude or semi-purified receptor-destroying enzyme has since been used as a standard reagent in influenza virus studies: further work in this field, together with increasing interest in the biological and chemical properties of compounds containing N-acetylneuraminic acid, have emphasized the need for the pure enzyme.