Reinigung und Charakterisierung der Neuraminidase aus Vibrio cholerae

Abstract

Neuraminidase was purified 50 000 times and a crystalline preparation was obtained. The most significant step in this procedure was the specific binding of the enzyme to its substrate which forms the immobile phase in a column chromatography. The enzyme sedimentated homogeneously with s20=1.3 S. The reaction kinetics of the enzyme was studied. The rate of hydrolysis for various substances was measured and the Michaelis constant was determined using stromata as substrate.