Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity

@article{Altmann1995KineticCO,
  title={Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity},
  author={Friedrich Altmann and Stefan Schweiszer and Christoph Friedrich Weber},
  journal={Glycoconjugate Journal},
  year={1995},
  volume={12},
  pages={84-93}
}
The initial velocities of hydrolysis of nineteen glycopeptides by peptide: N-glycosidase F and A were determined. Substrates were prepared from bovine fetuin, hen ovalbumin, pineapple stem bromelain, bovine fibrin and taka-amylase. From these glycopeptides, several variants with regard to peptide and carbohydrate structure were prepared and derivatized with dabsyl chloride, dansyl chloride or activated resorufin. Tyrosine containing glycopeptides were also used without an additional chromophore… CONTINUE READING

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