The glycopeptides of the mouse immunoglobulin A T15.
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 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.
Young
N M
NM
Division of Biological Sciences, National Research Council of Canada, Ottawa.
Jackson
G E
GE
Brisson
J R
JR
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D007070:Immunoglobulin A / Q000737:chemistry*; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D010206:Papain; D010434:Pepsin A; D010446:Peptide Fragments; D013329:Structure-Activity Relationship
D000596:Amino Acids; D006020:Glycopeptides; D007070:Immunoglobulin A; D007140:Immunoglobulin Fab Fragments; D010446:Peptide Fragments; D010206:Papain; D010434:Pepsin A