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N Morel

Publications and source records attributed to N Morel.

122 records · Page 7Linked to original sources
PubMed1977

Isolation of pure cholinergic nerve endings from Torpedo electric organ. Evaluation of their metabolic properties.

Pure cholinergic nerve endings (synaptosomes) were isolated from the electric organ of Torpedo by a rapid procedure. These synaptosomes are approximately 3 micron in diameter. They contain an occasional mitochondrion, numerous synaptic vesicles, and sometimes an active zone is observed. No postynaptic membrane attachment is found. This nerve ending fraction is extremely pure as shown by morphological controls and biochemical data. It is rich in choline acetyltransferase (450 nmol/h per mg protein) and acetylcholine (ACh) (130 nmol/mg protein). The isolated endings retain their cytoplasmic components and they synthesize ACh and are stable in vitro for several hours, as shown by biochemical measurements and morphological analysis.

Acetylcholine↗
PubMedDate not supplied

Acetylcholinesterase: C-terminal domains, molecular forms and functional localization.

Acetylcholinesterase (AChE) possesses short C-terminal peptides that are not necessary for catalytic activity. These peptides belong to different classes (R, H, T, S) and define the post-translational processing and targeting of the enzyme. In vertebrates, subunits of type H (AChEH) and of type T (AChET) are the most important: AChEH subunits produce glycolipid (GPI)-anchored dimers and AChET subunits produce hetero-oligomeric forms such as membrane-bound tetramers in the mammalian brain (containing a 20 kDa hydrophobic protein) and asymmetric collagen-tailed forms in neuromuscular junctions (containing a specific collagen, ColQ). The T peptide allows the formation of tetrameric assemblies with a proline-rich attachment domain (PRAD) of collagen ColQ. These complex molecular structures condition the functional localization of the enzyme in the supramolecular architecture of cholinergic synapses.

Acetylcholinesterase↗