[A study of hydrolysis of various synthetic peptides with gastrointestinal enzymes using thin-layer chromatography].

Hydrolysis in vitro of alpha- and epsilon-peptide bonds of synthetic amino acids and peptide substrates,--models of protein fragments, with digestive enzymes was studied. The kinetics of hydrolysis was studied by quantitative thin-layer chromatography followed by densitometric analysis of the chromatographic patterns. The rate constants of hydrolysis of Phe-Lys, Gly-Lys dipeptides and their epsilon-acetyl and epsilon-succinyl derivatives with leucine aminopeptidase and pancreatic enzymes were calculated. epsilon-Acyl residues of the substrates failed to split off under these conditions. The digestive enzymes hydrolysed the alpha-peptide bonds adjacent to the acylated lysine. Hydrolysis of epsilon-acetyl substrates proceeded faster as compared to epsilon-succinyl derivatives.