Abstract

Hexosaminidase A from liver or placenta can be converted to an enzyme that behaves like hexosaminidase B by either bacterial or cerebral neuraminidase preparations. Concurrent with this change increasing amounts of N-acetyl neuraminic acid are released into the reaction mixture. Therefore, two properties of hexosaminidase isozymes, heat lability and electrophoretic migration, are due to N-acetyl neuraminic acid content. This interconversion may have metabolic significance.

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