Ontology type: schema:ScholarlyArticle
2000-01
AUTHORSN. P. Arbatsky, L. M. Likhosherstov, M. V. Serebryakova, O. S. Brusov, V. N. Shibaev, V. A. Derevitskaya, N. K. Kochetkov
ABSTRACTBy the example of fetuin and a blood-group-specific mucin from porcine stomach, we showed that, under conditions of reductive degradation of glycoproteins with LiBH4-LiOH in 70% aqueoustert-butyl alcohol, the reduction and cleavage of amide bonds occur much faster than the simultaneous β-elimination of carbohydrate chainsO-linked with Ser and Thr residues of the peptide chain. The major degradation products containing theO-linked glycans are theO-glycosylated derivatives of 2-aminopropane-1,3-diol and 2-aminobutane-1,3-diol (the products of reduction of glycosylated Ser and Thr) and the glycopeptides containing 2–4 amino acid residues with reducedC-terminal amino acid. Seventeen homogeneousO-glycopeptides were isolated from the fetuin degradation products by ion-exchange and reversed-phase HPLC. Their structures were determined by MALDI-TOF mass spectrometry and by analyses for amino acids, amino alcohols, and carbohydrates. The application of the reaction for characterization ofO-glycans and localization ofO-glycosylation sites inO- andN,O-glycoproteins is discussed. More... »
PAGES45-53
http://scigraph.springernature.com/pub.10.1007/bf02758860
DOIhttp://dx.doi.org/10.1007/bf02758860
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