[Analysis of proteins and glycoproteins from adult bovine cerebellum. II. Quantitative separation by Con A Sepharose chromatography].
Soluble and insoluble glycoproteins from adult bovine cerebellum have been separated by affinity chromatography on ConA-Sepharose and analyzed by polyacrylamide gel electrophoresis I2% in presence of SDS. Soluble fraction represents 26% of total proteins. Within soluble and insoluble fractions 4.5% of proteins binds to ConA. Electropherograms of the soluble and insoluble fractions as well as of the proteins not absorbed on ConA-Sepharose, display a very complex pattern. Soluble fractions present many sharp bands in the region of molecular weight above 100 k. Heterogeneity is lesser in ConA-binding proteins. The contamination by Concanavalin A is considered. At present no definite conclusions can be drawn regarding the similarities existing between s.c. soluble and membrane-bound cerebral glycoproteins.
D000818:Animals; D002417:Cattle; D002531:Cerebellum / Q000032:analysis*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification*; D008970:Molecular Weight; D012685:Sepharose / Q000031:analogs & derivatives; D012995:Solubility
D006023:Glycoproteins; C028326:concanavalin A-sepharose; D012685:Sepharose
Analisi di proteine e glicoproteine del cervelletto di bovino adulto- Note II. Separazione quantitativa mediante colonna di ConA-Sefarosio.