作者: Edith Heilbronn
DOI: 10.1016/0006-3002(62)91002-8
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摘要: Abstract Purification of cholinesterase preparations previously obtained by ammonium sulfate fractionation horse serum has been studied means zone electrophoresis and chromatography. A method is described allowing a 10–15 fold purification in one step. preparation splitting 14·10−4 moles acetylcholine/h/mg dry wt. was isolated for further kinetic studies. This contained 3.2% sialic acid. After renewed the splitted 70·10−4 The behavior during chromatography indicates presence two components showing activity serum. So far, no difference their reactions with inhibitors substrates found.