The glycopeptides of the mouse immunoglobulin A T15: Mol.Immunol.

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Journal titleMol.Immunol.
Pages10831090; # of pages: 8
SubjectACID; Acids; ALPHA; amino acid; Amino Acid Sequence; Amino Acids; AMINO-ACID; analysis; Animals; Canada; Carbohydrate Sequence; chemistry; complex; COMPLEX-TYPE; COMPLEXES; Digestion; DOMAIN; FC-FRAGMENT; glycopeptide; Glycopeptides; Glycosylation; Iga; IgM; Immunoglobulin A; Immunoglobulins; Immunoglobulins,Fab; Mice; Molecular Sequence Data; Papain; Pepsin A; peptide; Peptide Fragments; Pronase; SITE; SITES; Structure-Activity Relationship
AbstractCleavage 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 alpha 3 domain were located by sequencing. The two glycopeptides were prepared from the Fab and C-terminal fragments by pronase digestion. The C alpha 1 glycopeptide at Asn 155 was complex type with alpha (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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AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberYOUNG1990
NPARC number9374990
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Record identifier6183f4e3-b0bd-4132-8f5f-aa3b22df720b
Record created2009-07-10
Record modified2016-05-09
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