Table 1.

Predominant Glycosylation Found in IgA Isolated from Human Saliva

Sample	Complex glycans (%)						Oligomannose (%)
	Predominant glycan		Terminal Sialylation		Terminal Galactosylation	Terminal Fucosylation
	GO	GOF	α2–3	Total
Patient 1, dimeric IgA	12.2	12.0	1.4	14.8	26.2	56.9	–
Patient 1, monomeric IgA	18.5	5.6	2.9	27.4	36.2	56.6	–
Patient 2, dimeric IgA	12.5	20.7	6.7	17.3	17.4	55.5	–
Patient 2, monomeric IgA	18.8	17.0	5.7	10.5	16.0	56.4	–
3.1 IgA1	43.7	–	30.4	51.0	0.5	1.1	2.1
3.1 IgA2	53.3	–	11.2	22.1	1.2	12.1	1.8
3.1 IgG1	40.3	1.2	–	–	57.2	58.6	–

Different recombinant isotypes of mAb 3.1 as well as IgA from two adult male Caucasians purified from saliva were run on SDS-PAGE to separate dimeric from monomeric forms. The corresponding gel bands were excised, and the N-linked glycans were released from the protein by PNGase digestion and further subjected to digestion with specific glycosylases (EndoH, α2–3,6,8 neuraminidase, β1,4-galactosidase, α-L-fucosidase, β-N-acetylglucosaminidase, α(1-2,3,6)-mannosidase). Differential analysis by HILIC-UPLC was then performed, and the percentages were determined by the sum of the areas under the specific peaks over the area under all peaks.