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4‐Methylumbelliferyl Lipase in Human and Mouse Brain: A Possible Localization in Myelin
Author(s) -
Tada Y.,
Sekiguchi S.,
Ito F.,
Eto Y.
Publication year - 1986
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.1471-4159.1986.tb12936.x
Subject(s) - lipase , myelin , biochemistry , chemistry , enzyme , substrate (aquarium) , chromatography , biology , central nervous system , endocrinology , ecology
4‐Methylumbelliferyl (4‐MU) lipase activity in human and mouse brain, measured with 4‐MU palmitate, was characterized with respect to effects of pH and detergents, and subcellular and myelin localization. Purified myelin isolated by Norton's procedure [ J. Neurochem. 21, 749–757 (1983)] contained higher specific activity of 4‐MU lipase, particularly in alkaline pH. Myelin lipase activity was markedly affected by the addition of different types of detergents, the amount of detergents added, and substrate. The optimal pH in myelin was bimodal—pH 4.5 and up to 8.0, respectively. These data indicate that myelin possesses 4‐MU lipase activity at alkaline pH, with lower levels at acidic pH.