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1: Biochem Mol Med. 1997 Jun;61(1):47-51.Click here to read Links

Comparison of the hydrolysis of the three types of natriuretic peptides by human kidney neutral endopeptidase 24.11.

Watanabe Y, Nakajima K, Shimamori Y, Fujimoto Y.

Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.

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.

PMID: 9232196 [PubMed - indexed for MEDLINE]