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β‐Glucosidase and β‐Galactosidase in Primary Cultures of Rat Astrocytes: Comparison to the Brain Enzymes
Author(s) -
Hof Liselotte,
Kimelberg Harold K.
Publication year - 1985
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.1471-4159.1985.tb07141.x
Subject(s) - enzyme , astrocyte , beta galactosidase , biochemistry , glycoside hydrolase , acid phosphatase , galactosidases , alkaline phosphatase , glucosidases , biology , chemistry , endocrinology , central nervous system , gene expression , gene
In primary astrocyte cultures β‐glucosidase (EC 3.2.1.21) and β‐galactosidase (EC 3.2.1.23) showed pH optima and K m values identical to rat brain enzymes, using methylumbelliferyl glycosides and labeled gluco‐and galactocerebrosides as substrates. The activities of both glycosidases increased in culture up to 3–4 weeks. In rat brain only galactosidase increased; glucosidase activity declined between 12–20 days after birth. The specific activities were two‐ to sixfold higher in astrocyte cultures than in rat brain. These activities were not due to uptake of enzymes from the growth medium. Secretion of β‐galactosidase, but not β‐glucosidase nor acid phosphatase could be demonstrated. These results support the suggestion of a degradative function for astrocytes in the brain.