title: [A study of hydrolysis of various synthetic peptides with gastrointestinal enzymes using thin-layer chromatography].
abstract: 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.
authors.forename: S M
authors.initials: SM
authors.lastname: Andreev
authors.forename: N A
authors.initials: NA
authors.lastname: Samoilova
authors.forename: S V
authors.initials: SV
authors.lastname: Rogozhin
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D002855:Chromatography, Thin Layer; D004064:Digestive System / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D007931:Leucyl Aminopeptidase / Q000378:metabolism; D010194:Pancreatin / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D010455:Peptides; D010194:Pancreatin; D007931:Leucyl Aminopeptidase
vernacular_title: Issledovanie gidroliza nekotorykh sinteticheskikh peptidov fermentami zheludochno-kishechnogo trakta metodom tonkosloĭnoĭ khromatografii.