| DOI | Trouver le DOI : https://doi.org/10.1016/0161-5890(90)90096-I |
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| Auteur | Rechercher : Young, N. Martin1; Rechercher : Jackson, Gail E.1; Rechercher : Brisson, Jean-Robert1 |
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| Affiliation | - Conseil national de recherches du Canada
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| Format | Texte, Article |
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| Sujet | 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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| Résumé | 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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| Date de publication | 1990-11-01 |
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| Maison d’édition | Elsevier |
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| Dans | |
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| Langue | anglais |
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| Identificateur | NRC-IBS-YOUNG1990 |
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| Numéro NPARC | 9374990 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 6183f4e3-b0bd-4132-8f5f-aa3b22df720b |
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| Enregistrement créé | 2009-07-10 |
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| Enregistrement modifié | 2020-03-17 |
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