Studies on bovine brain membrane-bound neuraminidase (sialidase).
1) Lipophilic ganglioside GD1a (IV3NeuAc, II3NeuAc-GgOse4-Cer) is taken up by the cell membranes and hydrolyzed faster by membrane-bound neuraminidase than are water soluble substrates of the enzyme. 2) The enzymic breakdown of ganglioside GD1a is enhanced by general anesthetics whereas the degradation of the hydrophilic substrate sialyllactitol is reduced by these same agents. 3) General anesthetics lower the microviscosity of membranes as indicated by studies of fluorescence depolarisation with the indicator 1,6-diphenylhexatrien. Decreased microviscosity can result in a higher lateral diffusion of ganglioside GD1a, increasing its interaction with membrane-bound neuraminidase. 4) In vitro studies indicate that the activity of membrane-bound neuraminidase on gangliosides of brain membranes is regulated by the viscosity of these membranes and their monosialoganglioside content.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D005732:Gangliosides; D006017:Glycolipids; D007700:Kinetics; D008081:Liposomes; D008861:Microsomes / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D013109:Sphingomyelins; D014316:Tritium
D005732:Gangliosides; D006017:Glycolipids; D008081:Liposomes; D013109:Sphingomyelins; D014316:Tritium; D011092:Polyethylene Glycols; D009439:Neuraminidase