中性内肽酶对脑钠肽的降解作用：通过质谱法确定的蛋白水解的物种特异性位点
Degradation of brain natriuretic peptide by neutral endopeptidase: species specific sites of proteolysis determined by mass spectrometry.
作者信息
Norman J A, Little D, Bolgar M, Di Donato G
机构信息
Department of Cardiovascular Biochemistry, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey.
出版信息
Biochem Biophys Res Commun. 1991 Feb 28;175(1):22-30. doi: 10.1016/s0006-291x(05)81194-5.
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 Arg8-Leu9 and Ser14-Leu15 bonds. Rat BNP was cleaved at the Arg23-Leu24 and Arg30-Leu31 bonds. Human BNP was cleaved at the Pro2-Lys3, Met4-Val5 and Arg17-Leu18 bonds. The Cys-Phe bond which is present in all species of BNP is not cleaved by NEP.
来自3个不同物种的脑钠肽（BNP）被中性内肽酶（NEP）切割，产物通过高效液相色谱法（HPLC）分离。通过快原子轰击或雾化辅助电喷雾质谱法鉴定新形成的产物，以阐明蛋白水解位点。猪BNP在Arg8-Leu9和Ser14-Leu15键处被切割。大鼠BNP在Arg23-Leu24和Arg30-Leu31键处被切割。人BNP在Pro2-Lys3、Met4-Val5和Arg17-Leu18键处被切割。所有物种的BNP中存在的Cys-Phe键不会被NEP切割。
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