DEGRADATION OF BRAIN NATRIURETIC PEPTIDE BY NEUTRAL ENDOPEPTIDASE - SPECIES-SPECIFIC SITES OF PROTEOLYSIS DETERMINED BY MASS-SPECTROMETRY
DEGRADATION OF BRAIN NATRIURETIC PEPTIDE BY NEUTRAL ENDOPEPTIDASE - SPECIES-SPECIFIC SITES OF PROTEOLYSIS DETERMINED BY MASS-SPECTROMETRY
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DOI：
10.1016/s0006-291x(05)81194-5
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发表时间：
1991-02-28
影响因子：
3.1
通讯作者：
DIDONATO, G
中科院分区：
文献类型：
--
作者：
NORMAN, JA;LITTLE, D;DIDONATO, G
用中性内肽酶（NEP）对3种不同物种的脑钠肽（BNP）进行裂解，并用高效液相色谱（HPLC）对产物进行分离。通过快速原子轰击或喷雾辅助电喷雾质谱法对新形成的产物进行鉴定，以阐明蛋白质水解的位点。猪BNP在arg8 - leu9和ser14 - leu15键上被切割。大鼠BNP在arg23 - leu24和arg30 - leu31键处断裂。人BNP在Pro2-Lys3、met4 - val5和arg17 - leu18键上被切割。存在于所有BNP物种中的Cys-Phe键不会被NEP切割。
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-Leu9and Ser14-Leu15bonds. Rat BNP was cleaved at the Arg23-Leu24and Arg30-Leu31bonds. Human BNP was cleaved at the Pro2-Lys3, Met4-Val5and Arg17-Leu18bonds. The Cys-Phe bond which is present in all species of BNP is not cleaved by NEP.