Affordable Access

Publisher Website

Degradation of brain natriuretic peptide by neutral endopeptidase: Species specific sites of proteolysis determined by mass spectrometry

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
175
Issue
1
Identifiers
DOI: 10.1016/s0006-291x(05)81194-5

Abstract

Brain natriuretic peptide (BNP) from 3 different species was cleaved by neutral endopeptidase (NEP) and the products separated by HPLC. The newly formed products were identified by fast atom bombardment or nebulizer-assisted electrospray mass spectrometry to elucidate the sites of proteolysis. Porcine BNP was cleaved at the Arg 8-Leu 9 and Ser 14-Leu 15 bonds. Rat BNP was cleaved at the Arg 23-Leu 24 and Arg 30-Leu 31 bonds. Human BNP was cleaved at the Pro 2-Lys 3, Met 4-Val 5 and Arg 17-Leu 18 bonds. The Cys-Phe bond which is present in all species of BNP is not cleaved by NEP.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments