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

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

Protein	Enzyme(s) used	Glycosylation site	¹⁸O deamidation	¹⁶O deamidation	Unmodified N- sequon	Glycosylation state
hPGHS-1	AspN + trypsin + GluC	N67	+	+	+	Variable^II-III / Yes^I
		N103 ¹	-	+	+	No
		N143	+	-	+	Variable^II-III / Yes^I
		N409	-	-	-	ND²
hPGHS-2/-1 chimera	AspN + trypsin	N53	+	+	+	No^II / Yes^I
		N103 ¹	-	+	+	No
		N143	+	-	-	Yes
		N409	+	-	-	Yes
hPGHS-2	trypsin	N53	+	+	+	No^II-IV / Yes^I
		N130	+	+	+	Variable^III-IV / Yes^I-II
		N396	+	+	+	Variable^III-IV / Yes^I-II
		N580	+	-	-	Yes
		N592 ¹	-	-	+	No

¹N-glycosylation sequons not glycosylated in native hPGHS proteins.
²no data.
^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.