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MOLECULAR PROPERTIES OF CHOLINE ACETYLTRANSFERASE FROM DIFFERENT SPECIES INVESTIGATED BY ISOELECTRIC FOCUSING AND ION EXCHANGE ADSORPTION
Author(s) -
MaltheSørenssen D.
Publication year - 1976
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.1471-4159.1976.tb04462.x-i1
Subject(s) - choline acetyltransferase , isoelectric point , choline , isoelectric focusing , chemistry , biochemistry , torpedo , acetyltransferase , enzyme , microbiology and biotechnology , biology , central nervous system , gene , endocrinology , acetylation , receptor , acetylcholine receptor
—The isoelectric point, surface charge and K m for choline of choline acetyltransferase from different species were determined. Choline acetyltransferase from mouse and monkey brain was resolved into three molecular forms with isoelectric points at 7·1, 7·5, 8·4 and 7·0, 7·35, 8·35 respectively, whereas choline acetyltransferase from the electric organ of Torpedo and from rabbit brain showed a molecular form with isoelectric point 6·6 and 6·9, respectively. With the exception of rabbit brain enzyme, there was a good correlation between the isoelectric points and surface charges of the different choline acetyltransferases. The K m 's for choline were 0·66, 0·88, 0·92 and 3·5 mM for monkey, mouse, rabbit and Torpedo choline acetyltransferase respectively. The separated molecular forms of mouse and monkey enzymes did not show any significant difference in their affinity for choline.