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  • Title: [Enzymatic properties of neuraminidase from corynebacterium diptherial].
    Author: Khorlin IIa, Vertiev VV, Ezepchuk IaM, Privalova IM, Kvaratskheliia LD.
    Journal: Biokhimiia; 1975; 40(4):819-23. PubMed ID: 812557.
    Abstract:
    Enzymatic properties of neuraminidase isolated from non-toxigenic strain C7 of diphteritic bacteria are studied. The enzyme has the pH optimum 5.5--6.0 in acetate buffer and the temperature optimum 38 degrees C. Neuraminidase has the highest substrate affinity to glycoproteins of equine blood serum, the lowest affinity--to 3-N-acetylneuraminosyllactose and ovomucin. The Km values was 4.3-10(-4) at optimal conditions under the hydrolysis of 3-N-acetylneuraminosyllactose, Vm was 0.05+/-0.02 muM NANA/hour/mg of protein. The following esters of N-glyconoyl-glycine were shown to be competitive inhibitors of neuraminidase: 1) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-arabinooctonic acid; 2) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-glucoheptodecanic acid; 3) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-galactonic acid; 4) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-gluconic acid, Ki values being 6.5-10(-4), 4.5-10(-4); 9.5-10(-4) and 7.1-(10-3) M, respectively.
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