Publications by authors named "Sangeeth Krisnanchettiar"
Article Synopsis
- The study focuses on using thermal-assisted partial acid hydrolysis to break down carbohydrate parts of N-glycosylated peptides in horseradish peroxidase (HRP), aiming to create oligosaccharide cleavage ladders for mass spectrometry analysis.
- Different concentrations of trifluoroacetic acid were employed at various temperatures to selectively hydrolyze oligosaccharide units while minimizing peptide bond decomposition, and various glycopeptides of HRP were tested.
- Findings revealed that fucose is the most easily cleaved oligosaccharide, with specific glycopeptides carrying distinct oligosaccharide structures, helping in identifying glycopeptides and their monosaccharide compositions.
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was used to detect biotinylated peptides captured by avidin functional affinity electrophoresis (AFAEP). Peptide samples loaded onto AFAEP were heated with sodium dodecyl sulfate to ensure that the peptides are negatively charged, and thus migrate electrophoretically toward the cathode through the embedded avidin zone in the middle of the gel. To detect the biotinylated peptides, the band containing the avidin-biotinylated peptide complexes was excised from a 7.
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