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  • Title: The specificity of beta-galactosidase in the degradation of gangliosides.
    Author: Suzuki K, Tanaka H, Yamanaka T, Van Damme O.
    Journal: Adv Exp Med Biol; 1980; 125():307-18. PubMed ID: 6767344.
    Abstract:
    Available evidence indicates that a least two genetically distinct acidic lysosomal beta-galactosidases are present in mammalian tissues. One of them, galactosylceramidase, is primarily responsible for degradation of galactosylceramide, galactosylsphingosine, and monogalactosyl-diglyceride, while the other, GM1-ganglioside beta-galactosidase, degrades GM1-ganglioside and asialo GM1-ganglioside. Lactosylceramide can be hydrolyzed by either of the two enzymes. These substrate specificities of the two beta-galactosidases can adequately explain the known findings in the two genetic beta-galactosidase deficiency diseases. The possibilities of the specific lactosylceramidase have not yet received the necessary independent confirmation.
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