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dc.contributor.authorKongsak Boonyapranaien_US
dc.contributor.authorHsien Yu Tsaien_US
dc.contributor.authorMiles Chih Ming Chenen_US
dc.contributor.authorSupawadee Sriyamen_US
dc.contributor.authorSupachok Sinchaikulen_US
dc.contributor.authorSuree Phutrakulen_US
dc.contributor.authorShui Tien Chenen_US
dc.description.abstractExtra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp. In this work, we demonstrated how differences of multimeric conformation alter the glycosylation of Hp. The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample. Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan. Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp. A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer. In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration. Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleGlycoproteomic analysis and molecular modeling of haptoglobin multimersen_US
article.volume32en_US Sinica Taiwanen_US Mai Universityen_US Taiwan Universityen_US University of Technology Lannaen_US
Appears in Collections:CMUL: Journal Articles

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