Studies on the glycoprotein component of (Na+-k+) atpase from guinea pig brain.
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.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003208:Concanavalin A / Q000494:pharmacology; D006023:Glycoproteins / Q000032:analysis*; D008297:Male; D008861:Microsomes / Q000201:enzymology; D009439:Neuraminidase; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis* / Q000037:antagonists & inhibitors
D006023:Glycoproteins; D003208:Concanavalin A; D009439:Neuraminidase; D000254:Sodium-Potassium-Exchanging ATPase