Polymorphism of acetylcholinesterase and identification of new molecular forms after sedimentation analysis.
Acetylcholinesterase (AChE) is composed of several distinct molecular forms, which are identified and partly resolved by velocity sedimentation analysis on sucrose gradients. We made the assumption that each AChE form sediments as a peak of activity with a gaussian shape in the continuous sucrose gradient. We experimentally demonstrate that the complex AChE profiles can be decomposed in gaussian distributions of separate molecular entities. We performed a high salt-detergent extraction of AChE from mouse skeletal muscle and isolated fractions enriched in each particular from. These fractions were then submitted to a second sedimentation, to assess the stability and to further characterize each AChE form. Then, we calculated the statistical significance level of each AChE form and identified up to 9 separate molecular specifies in mouse adult muscle. These forms are the major "4 S", "6.5 S", "10 S", "12 S" and "16 S" and minor molecular active components of AChE. These results suggest complex structural interactions between catalytic and non catalytic subunits of AChE and do not simply fit the tailed asymmetric globular model of AChE with six molecular species.
D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D002499:Centrifugation, Density Gradient; D007527:Isoenzymes; D051379:Mice; D009045:Motor Endplate / Q000201:enzymology; D009132:Muscles / Q000201:enzymology*
D007527:Isoenzymes; D000110:Acetylcholinesterase