C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry.
C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry.
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蛋白质 C 端测序。
DOI：
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发表时间：
1992
期刊：
影响因子：
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通讯作者：
H. Iwadate
中科院分区：
文献类型：
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作者：
A. Tsugita;K. Takamoto;M. Kamo;H. Iwadate
肽或蛋白质通过90%五氟丙酸或七氟丁酸的蒸气在90 ° C下水解不同的时间段。通过快速原子轰击和电喷雾电离质谱分析的水解产物混合物显示了一系列的C-末端连续降解分子离子。降解反应可能是由于在C-末端氨基酸处选择性形成恶唑酮环，然后水解除去C-末端氨基酸。主要的副反应是天冬氨酸残基C端和丝氨酸残基N端的肽键断裂。
Peptides or proteins were hydrolyzed by vapors of 90% pentafluoropropionic acid or heptafluorobutyric acid at 90 degrees C for various time periods. The hydrolyzate mixtures analyzed by both fast-atom-bombardment and electrospray ionization mass spectrometry showed a series of C-terminal successive degradation molecular ions. The degradation reaction may be due to the selective formation of an oxazolone ring at the C-terminal amino acid, followed by hydrolytic removal of the C-terminal amino acid. The major side reactions were cleavages of the peptide bonds at the C side of the internal aspartic acid residue and the N side of serine residue.