Proteolytic release of glycopeptides from glycoproteins transferred to nitrocellulose following gel electrophoresis.
To determine whether glycopeptides could be released from glycoproteins bound to nitrocellulose, the glycoproteins of murine mammary tumor virus (MuMTV) were radiolabeled by the periodate oxidation/tritiated sodium borohydride reduction technique and separated by gel electrophoresis followed by diffusion transfer. Pronase digestion of nitrocellulose filter strips containing labeled glycoproteins (gp55 or gp34) revealed a rapid release of glycopeptides, i.e., approximately total release within 4 h. The released glycopeptides were similar in size, as determined by molecular sieving chromatography, to glycopeptides obtained by proteolytic digestion of MuMTV glycoproteins from dried gel strips (A. Zilberstein et al., 1980, Cell 21, 417-427) or in solution (M. J. Yagi et al., 1978, Virology 91, 291-304).
Dion
A S
AS
Pomenti
A A
AA
D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis*; D008324:Mammary Tumor Virus, Mouse / Q000032:analysis; D010447:Peptide Hydrolases / Q000494:pharmacology; D014316:Tritium
D006020:Glycopeptides; D006023:Glycoproteins; D014316:Tritium; D003101:Collodion; D010447:Peptide Hydrolases