Protein Tyrosine Phosphorylation in Synaptic Vesicles

Protein tyrosine phosphorylation in purified synaptic vesicles from rat forebrain has been studied in the presence of Mn2+ and orthovanadate. High levels of endogenous protein tyrosine phosphorylation were observed. Four major phosphoproteins, with apparent molecular masses of 105, 94, 38, and 30 kD...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1988-02, Vol.85 (3), p.762-766
Hauptverfasser:	Pang, Dennis T., James K. T. Wang, Valtorta, Flavia, Benfenati, Fabio, Greengard, Paul
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkalies Animals Biological and medical sciences brain Brain Chemistry Cell physiology Forebrain Fundamental and applied biological sciences. Psychology Gels Glycoproteins - metabolism Immunoprecipitation Male Manganese - metabolism membrane proteins Membrane Proteins - metabolism Molecular and cellular biology Nerve Tissue Proteins - metabolism Nerves Neurotransmission Phosphates Phosphoamino acids Phosphoproteins Phosphoproteins - biosynthesis Phosphoproteins - isolation & purification Phosphorylation Protein-Tyrosine Kinases - metabolism Rats Rats, Inbred Strains synaptic vesicles Synaptic Vesicles - metabolism Synaptophysin Synaptosomes Synaptosomes - metabolism Vanadates - metabolism
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