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Differentiation-dependent changes of nicotinic synapse-associated proteins

MPG-Autoren
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Witzemann,  Veit
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Witzemann, V., Schmid, D., & Boustead, C. (1983). Differentiation-dependent changes of nicotinic synapse-associated proteins. European Journal of Biochemistry, 131(2), 235-245. doi:10.1111/j.1432-1033.1983.tb07255.x.


Zitierlink: http://hdl.handle.net/21.11116/0000-0000-E5AC-C
Zusammenfassung
Developmentally regulated changes were followed by analyzing the protein composition in vivo of the electric organ of Torpedo marmorata. A 45 000-Mr component, most likely a form of actin, is found to decrease during synaptogenesis, whereas a 43 000-Mr component increases significantly at later embryonic stages, to become the most abundant protein of electric organ. The 43 000-Mr polypeptides are heterogeneous in their solubilization properties and isoelectric points. Translation in vitro of mRNA isolated from embryonic electric organ shows that the appearance of these proteins during development is regulated by the amount of translatable mRNA available. The close correlation between the translatable amounts of mRNA in vitro and the protein synthesis observed in vivo during synaptogenesis suggests that the functional maturation of the electric organ is linked to the appearance of 43 000-Mr polypeptides.