[The use of 1H-NMR-spectroscopy for the study of peptide degradation by angiotensin-converting enzyme].
A new method for continuous registration of enzymatic hydrolysis of peptides involving 1H-NMR spectroscopy was developed. The advantages of the method were demonstrated, using dalargin (Tyr-D-Ala-Gly-Phe-Leu-Arg) hydrolysis catalyzed by human kidney angiotensin-converting enzyme as an example. It was shown that the maximal activity of the enzyme towards dalargin is observed at pH 7.8; Km is 0.35 mM. The enzyme is inhibited by the substrate (Kd = 0.55 mM). Cl- do not influence the catalytic activity of the enzyme with respect to dalargin. The stereospecificity of the angiotensin-converting enzyme towards dalargin diasteriomers was studied.
D004743:Enkephalin, Leucine / Q000031:analogs & derivatives / Q000032:analysis; D016308:Enkephalin, Leucine-2-Alanine / Q000031:analogs & derivatives*; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000032:analysis*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*
D010455:Peptides; D004743:Enkephalin, Leucine; D016308:Enkephalin, Leucine-2-Alanine; D007703:Peptidyl-Dipeptidase A; C040996:enkephalin-Leu, Ala(2)-Arg(6)-
Primenenie 1H-IaMR-spectroskopii dlia issledovaniia degradatsii peptidov angiotenzinprevrashchaiushchim fermentom.