Acetylcholinesterase: A useful marker for the isolation of sarcolemma from the bivalve (Modiolus demissus demissus) myocardium
Open Access
- 1 December 1978
- journal article
- research article
- Published by The Company of Biologists in Journal of Cell Science
- Vol. 34 (1), 193-208
- https://doi.org/10.1242/jcs.34.1.193
Abstract
The presence of cholinesterase activity in M. demissus hearts was demonstrated by light- and electron-microscopic histochemistry and by enzymic assay. The enzyme proved to be acetylcholinesterase (AChE) since acetylthiocholine was the preferred substrate, and eserine or BW284c51inhibited the enzyme activity, while isoOMPA was without effect. The AChE was localized and uniformly distributed along the cell surface membranes of the cardiac muscle cells. A fraction 8-fold enriched in AChE was isolated from pooled ventricles by a combination of differential and sucrose density gradient centrifugation. This sarcolemmal fraction contained little mitochondrial contamination as determined by electron microscopy and by succinate cytochrome c reductase activity. In addition, this fraction stained uniformly for AChE, indicating that it was free of other membrane types (for example sarcoplasmic reticulum which did not stain for ACHE). Therefore, this fraction contained purified cell surface membrane free of contamination by other membranous organelles.This publication has 30 references indexed in Scilit:
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