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Neuraminidase was found in nearly all strains of Pasteurella multocida, in some strains of P. haemolytica, but not in P. pseudotuberculosis. The enzyme of P. multocida is bound to the bacterial cell. It is inducible by N-acetyl-D-mannosamine and by free and bound sialic acid. After solubilization it has a molecular weight of about 250000, a pH optimum = 6.0, and a Michaelis constant Km = 2 ⨯ 10-4 M when 3’-sialyllactose is used as substrate.
N-acetylneuraminate pyruvate-lyase activity present in Pasteurella multocida is higher in the cell-free culture medium than in the bacterium.
It is suggested that the stimulating effect of blood sera on the production of neuraminidase by Pasteurella multocida is due to the delayed release of the inducer N-acetyl-D-mannosamine.
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