After initial profiling of saliva samples by SDS gel underwent trypsin in solution digestion...Those digested peptides again underwent SDS gel to check whether the peptides digested or not but the result shows only high molecular weight proteins get digested and the low molecular weight proteins got undigested...Kind explain and elaborate the reason regarding this ??
Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, so it possibility that the high MW proteins digested because the contains lysine or arginine in their primary structure will the short peptides do not contain carboxyl side of the amino acids lysine or arginine.
@jasim Al-saaldi....In order to get digestion of low molecular weight proteins by trypsin ...what steps we will go ???
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