Abstract
In this study an attempt was made to elucidate the possible mechanism of the brain microsomal (Na+-K+)ATPase inhibition based on the assumption that glycoprotein part of the enzyme is exposed on the outer membrane surface. In our experiments the modification with concanavalin A of sugar end groups exposed by neuraminidase treatment resulted in a significant decrease of the brain (Na+-K+)ATPase activity. The percentage of the enzyme inhibition by concanavalin A binding to the neuraminidase-treated preparation corresponds to the amount of liberated sialic acids. The modification of the glycoprotein part of the brain (Na+-K+)ATPase complex by neuraminidase and concanavalin A treatments did not affect K+-nitrophenylphosphatase activity.
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Rossowska, M. Studies on the glycoprotein component of (Na+-K+)ATPase from guinea pig brain. Neurochem Res 4, 723–729 (1979). https://doi.org/10.1007/BF00964469
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DOI: https://doi.org/10.1007/BF00964469