Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat
| Autor: | George B. Koelle, Daniel Eugene, Genevieve Boulla, Jean Massoulié, Mariarosa A. B. Melone |
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| Přispěvatelé: | Koelle, Gb, Massoulie, J, Eugene, D, Melone, Mariarosa Anna Beatrice, Boulla, G. |
| Rok vydání: | 1987 |
| Předmět: |
Superior cervical ganglion
Stellate Ganglion Enolase Biology Isozyme chemistry.chemical_compound Dorsal root ganglion Ganglia Spinal medicine Animals Cholinesterases Butyrylcholinesterase Ganglia Sympathetic Multidisciplinary L-Lactate Dehydrogenase Ciliary ganglion Acetylcholinesterase Isoenzymes medicine.anatomical_structure Biochemistry chemistry Organ Specificity Phosphopyruvate Hydratase Stellate ganglion Cats Caudate Nucleus Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the alpha alpha, alpha gamma, and gamma gamma enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical findings. The results are consistent with the premise that the G1 (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites. |
| Databáze: | OpenAIRE |
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