The ATPase of cholinergic synaptic vesicles is associated with sugars |
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| Affiliation: | 1. European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstraße 1, 69117, Heidelberg, Germany;2. Candidate for Joint PhD Degree from EMBL and Heidelberg University, Faculty of Biosciences, Germany;3. Ernst-Ruska Centre for Microscopy and Spectroscopy with Electrons (ER-C-3/Structural Biology), Forschungszentrum Jülich, 52425, Jülich, Germany;4. JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, 52425, Jülich, Germany;5. Chemistry Department, Heinrich Heine University Düsseldorf, Düsseldorf, Germany;1. Department of Pharmacology, University of Washington, Seattle, WA 98195, USA;2. Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China;3. Molecular Medicine, Hospital for Sick Children, Toronto, ON M5G 0A4, Canada;4. Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada;5. Division of General Internal Medicine, Department of Medicine, University of Washington, Seattle, WA 98195, USA;6. Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA;1. Shanghai Institute of Pharmaceutical Industry Co., Ltd., China State Institute of Pharmaceutical Industry, Shanghai 201203, China;2. National Key Laboratory of Lead Druggability Research, Shanghai Institute of Pharmaceutical Industry Co. Ltd., Shanghai 201203, China;3. School of Pharmacy, Shanghai Jiao Tong University, Shanghai 200240, China |
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| Abstract: | The ATPase in synaptic vesicles isolated from Torpedo californica electric organ can be nearly completely solubilized in octaethyleneglycoldodecyl ether containing buffer where it is stable only in a narrow pH range around neutrality. Solubilized ATPase adsorbs to Sepharose columns containing covalently linked Triticum vulgaris, Concanavalin A, Glycine max, Dolichos biflorus, Lens culinaris or Pisum sativum lectins in a manner responding to cognate sugar block or enzymatic deglycosylation in most cases. However, reproducible elution of adsorbed ATPase activity with cognate sugars could not be obtained. It is concluded that the cholinergic synaptic vesicle ATPase is a glycoprotein or it interacts with glycolipid. |
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