Reinigung und Charakterisierung der Neuraminidase aus Vibrio cholerae

Abstract

Neuramidinase was purified and concentrated to 50,000 times the amount in the original filtrate and a crystalline preparation was obtained. The most significant step in the procedure was the specific binding of the enzyme to its substrate which forms the immobile phase in column chromatography. The enzyme sedimented homogeneously with S 2O = 1.3 S. The reaction kinetics of the enzyme were studied. The rate of hydrolysis for various substances was measured and the Michaelis constant was determined using stromata as substrate.