Epstein-Barr antibodies in suspected nasopharyngeal carcinoma.
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Biomedical subjects
Publications and source records attributed to S K Chan.
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The complete amino acid sequence of a CNBr-fragment from human alpha1-protease inhibitor has been determined and is shown below. The peptide consists of 109 amino acid residues with 1 oligosaccharide unit. The 2 glutamic acid residues which have previously been shown to be substituted by lysine in the Z and by valine in the S mutant proteins are both located in this CNBr fragment. (formula: see text).
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Two glycopeptides present in equal amounts were isolated from a pronase digest of alpha1-protease inhibitor of human plasma by gel filtration on Sephadex G-50 and chromatography on DEAE-cellulose. The carbohydrate side chains in both glycopeptides are linked through asparaginyl residues. The glycopeptides were digested sequentially with specific glycosidases; and after each step, the released sugars as well as the composition of the residual peptides were determined. The linear structures of these glycopeptides deduced from these data are shown below. Based on the total carbohydrate content of the intact protein and with these structural data, it is postulated that 4 oligosaccharide units are attached to 1 molecule of the protein; 2 of these were represented as in Equation 1, the other 2 as in Equation 2.
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