https://www.selleckchem.com/CDK.html
The least efficient substrate for trypsin-catalysed hydrolysis was the acidified, intact protein with a specificity constant (kcat/Km) nearly five times lower than that of the acidified, pepsin-hydrolysate. Our results illustrate the synergy between pepsin and trypsin hydrolysis, and indicate that gastric hydrolysis increases the efficiency of the subsequent trypsin-catalysed hydrolysis of a model protein in the small intestine.For large-scale analysis of complex protein mixtures, liquid chromatography - tandem mass spectrometry (LC-MS/MS) has been
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