Identification of enzymatically produced peptide fragments by liquid chromatography and mass spectrometry.
R Baranowski, C Westenfelder, B L Currie
Index: Anal. Biochem. 121(1) , 97-102, (1982)
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Abstract
The qualitative and quantitative determination of peptide fragments of angiotensin I generated by rat lung dipeptidyl carboxypeptidase (angiotensin converting enzyme, EC 3.4.15.1) is described. Enzymatically formed peptide fragments, after derivatization with fluorescamine, were separated and isolated by reverse-phase high-performance liquid chromatography. The recovered fluorescamine derivative of histidyl-leucine was then further identified by mass spectrometry. It is anticipated that this approach would be widely applicable to other enzyme systems.
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