The use of hydrolytic enzymes and multi-stage tandem mass spectrometry to analyze pyridoxal phosphate-modified peptides
| Autor: | Phil Andrews, Eric S. Simon |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Proteolysis
Biophysics chemical and pharmacologic phenomena Mass spectrometry Tandem mass spectrometry 01 natural sciences Biochemistry Peptide Mapping 03 medical and health sciences chemistry.chemical_compound Peptide mass fingerprinting immune system diseases Tandem Mass Spectrometry Amide medicine Pyridoxal phosphate Molecular Biology Peptide sequence 030304 developmental biology chemistry.chemical_classification 0303 health sciences medicine.diagnostic_test 010401 analytical chemistry Cell Biology Alkaline Phosphatase nervous system diseases 0104 chemical sciences Enzyme chemistry Pyridoxal Phosphate lipids (amino acids peptides and proteins) Peptides |
| Zdroj: | Analytical biochemistry. 581 |
| ISSN: | 1096-0309 |
| Popis: | A previous approach was established that allowed direct identification of pyridoxal-5ˊ-phosphate (PLP) bonding sites in proteins using mass spectrometry after tryptic proteolysis. The approach required peptide mass fingerprinting owing to suppressed amide backbone fragmentation in favor of side-chain elimination of diagnostic product ions from PLP-derivatized lysyl residues. While sufficient for purified proteins, unambiguous sequence determination is needed to assign PLP bonding sites in unknown proteins in complex mixtures. Here, we describe the use of hydrolytic enzymes and multi-stage tandem mass spectrometry to elucidate the amino acid sequence and PLP bonding site in PLP-modified peptides. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect