Purification and Characterization of P<sub>400</sub> Protein, a Glycoprotein Characteristic of Purkinje Cell, from Mouse Cerebellum

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<jats:p><jats:bold>Abstract: </jats:bold> P<jats:sub>400</jats:sub> protein is a concanavalin A (Con A)‐binding, 250–kilodalton glycoprotein characteristic of cerebellum. Extraction conditions for P<jats:sub>400</jats:sub> protein were investigated, and complete solubilization of P<jats:sub>400</jats:sub> protein from a submicrosomal fraction (P31 fraction) of mouse cerebellum was attained by the combination of 4% Zwittergent 3–14 and 4 <jats:italic>M</jats:italic> guanidinium chloride. The solubilized P400 protein was purified using Sepharose CL‐4B and Con A‐Sepharose chromatography. A monoclonal antibody (18A10) was prepared against P<jats:sub>400</jats:sub> protein. Endo‐β‐<jats:italic>N</jats:italic>‐acetylglucosaminidase F digestion of P<jats:sub>400</jats:sub> protein revealed that P<jats:sub>400</jats:sub> protein has a small number of asparagine‐linked oligosaccharide chains and that the epitope that is recognized by 18A10 monoclonal antibody is not on the asparagine‐linked oligosaccharide portion. Tissue distribution of P<jats:sub>400</jats:sub> protein was investigated by immunoblot analysis using 18A10 monoclonal antibody. P<jats:sub>400</jats:sub> protein was abundant in the cerebellum, but a very small amount of P400 protein or related antigen was also detected in other parts of the nervous system and in nonneural tissues. Immunohis‐tochemical studies indicated that P<jats:sub>400</jats:sub> protein was distributed abundantly in the soma, the dendritic arborization, and the axon of the Purkinje cell. No immunoreaction was observed in the other types of cells.</jats:p>

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