Jan Jędrzejczyk

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The 'heavy', collagen-tailed form of acetylcholinesterase (AChE), having a s(0)20,w of 16S in mammals, occurs at vertebrate muscle endplates and has been widely regarded as a marker of neuronal influence on muscle in vivo. However, an interesting exception has been described by Bacou et al., in a previous report in Nature. They found, in a slow-twitch(More)
Individual motor endplates in the skeletal muscles of chickens genetically homozygous for muscular dystrophy have been compared with those in normal chickens. Measurements were made there, by specific autoradiographic techniques, of the numbers of total cholinesterase-like molecules and of acetylcholinesterase molecules. The acetylcholinesterase is(More)
Individual endplates were micro-dissected from chicken fast-twitch muscle, and the molecular forms of acetylcholinesterase and of pseudocholinesterase therein, identified by their sedimentation coefficients, were analysed directly. The forms actually present at the endplate, and those that are non-synaptic, were established. This analysis was also extended(More)
Chicken muscles offer several significant advantages for the use of cholinesterase as a marker of nerve-muscle interactions. A series of molecular forms of chicken muscle acetylcholinesterase (AChE), and likewise of pseudocholinesterase (psi ChE), has been defined. The form of AChE inside the endplates of fast-twitch muscle is H2c (20 S), with a collagenous(More)
Molecular forms of acetylcholinesterase and pseudocholinesterase were analyzed directly in the micro-dissected individual endplates of a slow-tonic chicken muscle. The major form in the endplate is the L2(6.5 S) form, while the collagen-tailed H2c (20 S) form, normally considered to be the synaptic form, is a very minor component, in contrast to its(More)