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A particulate enzyme that catalyzes the hydrolysis of N-acetylneuraminic acid from N-acetylgalactosaminyl (N-acetylneuraminosyl)galactosylglucosylceramide (Tay-Sachs ganglioside, Gm2) has been shown in various tissues of the rat. The products of the reaction are N-acetylneuraminic acid and N-acetylgalactosaminylgalactosylglucosylceramide. Preparations from the small intestine were used to investigate the properties of this enzyme. It is tightly particle-bound and unstable to a variety of physical treatments. Optimal activity occurs at pH 5.0. The reaction is inhibited by sodium taurocholate, Triton X-100, p-chloromercuribenzenesulfonate, and certain cations.
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Kolodny et al. (1971) studied this question.
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