Abstract
Sodium ion addition of 20 naturally occurring amino acids was investigated by triple quadruple tandem mass spectrometry. Results showed that most amino acids had extraordinarily weak force for non-covalent binding to sodium ion, while proline and phenylalanine easily captured sodium ion from solvents. By tandem mass spectrometry “sequence docking” method on Q-TOF2 (Waters, USA), full amino acid sequence of C-terminal peptide of acidic fibroblast growth factor was analyzed and it was confirmed that the adding site of sodium ion was proline (6Pro). Sodium ion-addition peaks in peptide mass fingerprinting (PMF) apparently decreased after adding 1% formic acid. The peptide sequence without sodium ion-addition and the sequence gap were determined using de novo technology, which was the same as the sequence of sodium ion-addition peptide.
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