PMID: PMC7108604-1-2

 

    Legend: Gene, Sites

Title : Isolation of glycopeptides

Abstract :
  1. Since SDS displayed several additional, radiolabeled protein bands, immunoprecipitated VE-cadherin samples were preparatively separated by SDS-PAGE, and bands containing VE-cadherin were excised (I in Figure 1)
  2. In order to avoid loss of material when eluting the whole glycoprotein , an in-gel proteolytic digestion was performed, after which radioactive glycopeptides could be easily eluted from the gel pieces
  3. From the known amino acid sequence of the glycoprotein (Suzuki ; Breviario et al., 1995), it could be deduced that treatment with trypsin would generate a glycopeptide resistant to peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidase F ( PNGase F) (Tarentino et al., 1985)
  4. Therefore, Asp-N endoproteinase from Pseudomonas fragi mutant was used instead
  5. In total, a glycopeptide preparation was obtained comprising about 105 cpm of incorporated 3H radioactivity
  6. As a control, unstained gel segments (II in Figure 1) were equally treated and eluted
  7. However, no radioactivity could be detected in the respective supernatants
Output (sent_index, trigger, protein, sugar, site):
  • 0. glycopeptides, , -, -, glycopeptides
  • 2. glycopeptides, , -, -, glycopeptides
  • 2. glycoprotein, , glycoprotein, -, -
  • 3. glycopeptide, , -, -, glycopeptide
  • 3. glycoprotein, , glycoprotein, -, -
  • 5. glycopeptide, , -, -, glycopeptide
Output(Part-Of) (sent_index, protein, site):
  • 3. glycoprotein, sequence
*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

 

Protein NCBI ID SENTENCE INDEX