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

作者: Jon A. Norman , Deborah Little , Mark Bolgar , Gerald Di Donato

DOI: 10.1016/S0006-291X(05)81194-5

关键词: Cleavage (embryo)Brain natriuretic peptideStereochemistryProteolysisChemistryBiochemistryFast atom bombardmentMass spectrometryNeprilysinEnzymeEndopeptidase

摘要: Brain natriuretic peptide (BNP) from 3 different species was cleaved by neutral endopeptidase (NEP) and the products separated HPLC. The newly formed were identified fast atom bombardment or nebulizer-assisted electrospray mass spectrometry to elucidate sites of proteolysis. Porcine BNP at Arg8-Leu9 Ser14-Leu15 bonds. Rat Arg23-Leu24 Arg30-Leu31 Human Pro2-Lys3, Met4-Val5 Arg17-Leu18 Cys-Phe bond which is present in all not NEP.

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