The glycopeptides of the mouse immunoglobulin A T15

Mol Immunol. 1990 Nov;27(11):1083-90. doi: 10.1016/0161-5890(90)90096-i.

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 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.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Carbohydrate Sequence
  • Glycopeptides / chemistry*
  • Glycosylation
  • Immunoglobulin A / chemistry*
  • Immunoglobulin Fab Fragments / chemistry
  • Mice
  • Molecular Sequence Data
  • Papain
  • Pepsin A
  • Peptide Fragments
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Glycopeptides
  • Immunoglobulin A
  • Immunoglobulin Fab Fragments
  • Peptide Fragments
  • Papain
  • Pepsin A