Electron microscopic study of concanavalin A binding to membranes of the Golgi complex.
Binding of Concanavalin A to the Golgi complex and the resultant effect on intramembrane particles and enzyme activity has been studied with Golgi-rich fractions isolated from rat liver. Con A binds mainly to the tubular network of the Golgi complex and, to a lesser extent, the peripheral regions of the cisternae. Interaction of Con A with Golgi membranes is accompanied by aggregation of intramembrane particles reflecting increased membrane fluidity. Enhancement of galactosyl transferase, membrane bound in the Golgi complex, also occurs with Con A binding.
D000818:Animals; D001665:Binding Sites; D003208:Concanavalin A / Q000378:metabolism*; D005293:Ferritins / Q000378:metabolism; D005700:Galactosyltransferases / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D008099:Liver / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D051381:Rats; D013347:Subcellular Fractions
D003208:Concanavalin A; D005293:Ferritins; D005700:Galactosyltransferases