Comparison of the Hydrolysis of the Three Types of Natriuretic Peptides by Human Kidney Neutral Endopeptidase 24.11
The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at...
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Veröffentlicht in: | Biochemical and molecular medicine 1997-06, Vol.61 (1), p.47-51 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at the beginning of its ring structure. Analysis of the cleavage sites of each peptide indicated that the initial cleavage site of hCNP-22 is analogous to that of hANP-28. The Cys-Phe bond of hBNP-32 was insensitive to this enzymatic cleavage. We speculate that the stability of hBNP-32 may result from the insusceptibility of its Cys-Phe bond at the beginning of the ring structure. |
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ISSN: | 1077-3150 1095-5577 |
DOI: | 10.1006/bmme.1997.2584 |