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ACETYLCHOLINESTERASE IN MOUSE BRAIN, ERYTHROCYTES AND MUSCLE
Author(s) -
Adamson Eileen D.
Publication year - 1977
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.1471-4159.1977.tb10432.x
Subject(s) - sephadex , acetylcholinesterase , enzyme , size exclusion chromatography , chemistry , chromatography , affinity chromatography , biochemistry , gel electrophoresis , labelling , antibody , biology , immunology
— The properties of the enzyme acetylcholinesterase (EC 3.1.1.7) from mouse brain, erythrocytes and muscle were investigated. The enzymes were examined by gel filtration in Sephadex G‐200, polyac‐rylamide gel electrophoresis, immunological reactions, active‐site labelling with tritiated di‐isopropyl‐phosphorofluoridate and also their kinetic properties were compared. All three enzymes appeared to have a single active small mol. wt. component of 80,000 to 82,000 which produced higher mol. wt. forms by aggregation. The partial purification of the enzyme from brain was achieved by affinity chromatography and this product was used to prepare antibodies. The purified immunoglobulin was shown to react with all three enzymes.