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Changes in Particulate Neuraminidase Activity During Normal and Staggerer Mutant Mouse Development
Author(s) -
Wille Wolfgang,
Trenkner Ekkhart
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb00475.x
Subject(s) - neuraminidase , cerebellum , cerebrum , biology , endocrinology , enzyme , medicine , enzyme assay , biochemistry , chemistry , central nervous system
The activity of particulate neuraminidase (sialidase, EC 3.2.1.18) in wild‐type mice and the neurological mutant Staggerer was studied during development. Peak activity of this enzyme was observed at postnatal day 3 (P3) in three tissues of normal mice: cerebellum, cerebrum, and liver. In Staggerer, however, neuraminidase peak activity was observed at P27 in the cerebellum, whereas the activity was close to normal in Staggerer cerebrum and liver. Activities of other glycosidases in Staggerer (α‐glucosidase (pH 3.7), α‐ glucosidase (pH 6.0), N ‐acetyl‐β‐hexosaminidase, β‐glucosidase, and β‐galactosidase) did not show significant variation compared with wild‐type at P27 in any of the three tissues. This indicates that the late activity peak of particulate neuraminidase activity in the Staggerer cerebellum is neuraminidase‐specific and not due to a general increase of lysosomal enzymes.

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