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heterogeneity of strongostrong-glycosylation in the hinge region of human.pdf

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heterogeneity of strongostrong-glycosylation in the hinge region of human

Molecular Immunology 37 (2000) 1047–1056 /locate/molimm Heterogeneity of O-glycosylation in the hinge region of human IgA1 Jan Novak a,*, Milan Tomana b, Mogens Kilian c, Lori Coward d, Rose Kulhavy a, Stephen Barnes d,e, Jiri Mestecky a,b a Department of Microbiology, 845 19th St. S., BBRB 734, Uniersity of Alabama at Birmingham, Birmingham, AL 35294, USA b Department of Medicine, Diision of Clinical Immunology and Rheumatology, Uniersity of Alabama at Birmingham, Birmingham, AL 35294, USA c Department of Medical Microbiology and Immunology, Uniersity of Aarhus, Bartholin Building, DK -8000 Aarhus C, Denmark d Mass Spectrometry Shared Facility, Uniersity of Alabama at Birmingham, Birmingham, AL 35294, USA e Department of Pharmacology and Toxicology, Uniersity of Alabama at Birmingham, Birmingham, AL 35294, USA Received 28 November 2000; accepted 14 March 2001 Abstract Matrix-assisted laser desorption ionization time-of-ﬂight (MALDI-TOF) mass spectrometry was applied to studies of the molecular heterogeneity of desialylated human IgA1 hinge region glycopeptides released with two IgA1 proteases. Typically, the hinge region of an 1 chain contains three to ﬁve O-linked glycan chains. Variants of the hinge region peptides released from IgA1(Kni) myeloma protein carrying 0, 1, 2, or 3 GalNAc residues were observed in the mas