Isolation of sarcolemma acetylcholinesterase fractions by gel-filtration through Sepharose 2B
Diadiusha, G.P.; Lesnaia, L.I.
Biokhimiia 43(3): 516-524
1978
ISSN/ISBN: 0320-9725 PMID: 656488 Document Number: 137712
Gel-filtration of 0,6 M NaCl and 0,6 M NaCl--0,1% Triton X-100 extracts of freshly isolated sarcolemma through Sepharose 2B (1,5 X 72 cm) has revealed one symmetric peak of acetylcholinesterase activity containing phospholipid and cholesterol, moving faster than fibrinogen and tyreoglobulin. The acetylcholinesterase fraction is substantially separated from other extract proteins. Gel-filtration of extracts from long-store, treated by ultrasound or high concentration of detergent sarcolemma has revealed some peaks of acetylcholinesterase activity, which may be suggested to be degraded forms of the complex high molecular weight structure. All species of acetylcholinesterase are converted by treatment with trypsin to a form moving upon gel-filtration with enzyme-marker catalase. The microsome extracts contain only the form moving with catalase.