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.
[Analysis of proteins and glycoproteins from adult bovine cerebellum. II. Quantitative separation by Con A Sepharose chromatography]
CORSI, Patrizia;GENNARINI, Gianfranco;RUCCIA, DOMENICO;VITIELLO, Francesco;DI BENEDETTA, Carlo
1980-01-01
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
