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 wa...

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Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 52; no. 2; p. 311
Main Authors:	Sakharov, I Iu, Isakova, O L, Sepetov, N F, Bespalova, Zh D, Ruuge, E K
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-02-1987
Subjects:	Enkephalin, Leucine - analogs & derivatives Enkephalin, Leucine - analysis Enkephalin, Leucine-2-Alanine - analogs & derivatives Humans Hydrolysis In Vitro Techniques Kidney - enzymology Kinetics Magnetic Resonance Spectroscopy Peptides - analysis Peptidyl-Dipeptidase A - metabolism
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Summary:	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.
ISSN:	0320-9725