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Acetylcholinesterase in Mouse Neuroblastoma Cells: Intracellular and Released Enzyme
Author(s) -
Kimhi Yosef,
Mahler Alexandra,
Saya Danielle
Publication year - 1980
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.1471-4159.1980.tb11180.x
Subject(s) - intracellular , acetylcholinesterase , extracellular , enzyme , biochemistry , polyacrylamide , polyacrylamide gel electrophoresis , biology , chemistry , microbiology and biotechnology
Mouse neuroblastoma cells in cultures release acetylcholinesterase into the growth medium. The released enzyme, as well as the intracellular activity, separate on a density gradient into two molecular forms, sedimenting as 4.5S and 10.5S entities. The relative amounts of these forms are different in the two cases: whereas the slower sedimenting form is the major one in the cellular extract, the 10.5S form predominates in the released activity. The cellular and released proteins were labelled by [ 3 H]diisopropylphosphofluoridate and analysed on polyacrylamide‐SDS gels. The results suggest that the intracellular as well as the extracellular molecules are oligomers of similar subunits.