| DOI | Resolve DOI: https://doi.org/10.1016/0161-5890(90)90096-I |
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| Author | Search for: Young, N. Martin1; Search for: Jackson, Gail E.1; Search for: Brisson, Jean-Robert1 |
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| Affiliation | - National Research Council of Canada
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| Format | Text, Article |
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| Subject | acid; alpha; amino acid; amino acid sequence; amino-acid; carbohydrate sequence; complex-type; digestion; domain; fc-fragment; glycopeptide; glycosylation; Iga; IgM; immunoglobulin A; immunoglobulins, Fab; mice; molecular sequence data; papain; pepsin a; peptide fragments; pronase; site; structure-activity relationship |
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| Abstract | Cleavage of mouse IgA T15 with papain yielded (a) a glycosylated Fab fragment, (b) a non-glycosylated Fc fragment and (c) a glycosylated C-terminal peptide. The cleavage sites at the hinge and at the end of the C α 3 domain were located by sequencing. The two glycopeptides were prepared from the Fab and C-terminal fragments by pronase digestion. The C α 1 glycopeptide at Asn 155 was complex type with α (1-3)galactose terminal groups, and closely resembled the Asn 171 glycopeptide of mouse IgM (Anderson et al. (1985) Arch. Biochem. Biophys. 243, 605-618). In contrast, the C-terminal glycopeptide at Asn 446 was entirely different from the corresponding IgM glycopeptide, being complex rather than high-mannose type |
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| Publication date | 1990-11-01 |
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| Publisher | Elsevier |
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| In | |
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| Language | English |
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| Identifier | NRC-IBS-YOUNG1990 |
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| NPARC number | 9374990 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 6183f4e3-b0bd-4132-8f5f-aa3b22df720b |
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| Record created | 2009-07-10 |
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| Record modified | 2020-03-17 |
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