Post-translational modifications in cartilage oligomeric matrix protein. Characterization of the N-linked oligosaccharides by matrix-assisted laser desorption ionization time-of-flight mass spectrometry.

@article{Zaia1997PosttranslationalMI,
  title={Post-translational modifications in cartilage oligomeric matrix protein. Characterization of the N-linked oligosaccharides by matrix-assisted laser desorption ionization time-of-flight mass spectrometry.},
  author={Joseph Zaia and Raymond E. Boynton and Alan Mcintosh and Daniel R. Marshak and H. K. Olsson and Dick Heineg{\aa}rd and F Barry},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 22},
  pages={14120-6}
}
Analysis of the carboxymethylated subunit of human cartilage oligomeric matrix protein (COMP) by matrix-assisted laser desorption time-of-flight mass spectrometry indicated a protonated molecular mass of 86949 +/- 149 Da, compared with 83547.0 Da calculated from the sequence. Treatment with N-glycanase caused a reduction in mass of 3571 +/- 219 Da, but there was no loss of mass after treatment with O-glycanase or neuraminidase. Peptides containing two putative sites of N-glycosylation were… CONTINUE READING
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