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Table 2 Mass-spectrometric analysis of the N -glycosylation patterns of hPGHS proteins

From: N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris

Protein Enzyme(s) used Glycosylation site 18O deamidation 16O deamidation Unmodified N- sequon Glycosylation state
hPGHS-1 AspN + trypsin + GluC N67 + + + VariableII-III / YesI
N103 1 - + + No
N143 + - + VariableII-III / YesI
N409 - - - ND2
hPGHS-2/-1 chimera AspN + trypsin N53 + + + NoII / YesI
N103 1 - + + No
N143 + - - Yes
N409 + - - Yes
hPGHS-2 trypsin N53 + + + NoII-IV / YesI
N130 + + + VariableIII-IV / YesI-II
N396 + + + VariableIII-IV / YesI-II
N580 + - - Yes
N592 1 - - + No
  1. 1N-glycosylation sequons not glycosylated in native hPGHS proteins.
  2. 2no data.
  3. I-IVhPGHS glycoforms, whereas I marks the protein with the highest molecular weight. If not depicted, the glycosylation state of the sequon was the same among all the glycoforms subjected to analysis.