[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.
Andreev
S M
SM
Samoilova
N A
NA
Rogozhin
S V
SV
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
D000596:Amino Acids; D010455:Peptides; D010194:Pancreatin; D007931:Leucyl Aminopeptidase
Issledovanie gidroliza nekotorykh sinteticheskikh peptidov fermentami zheludochno-kishechnogo trakta metodom tonkosloĭnoĭ khromatografii.