TABLE 1.
Endo-LysC peptide (residues) | Number of Asn residues in the peptide | Amount of Asn → Sera |
---|---|---|
% | ||
Antibody A, light chain | ||
L1 (1–33) | 0 | |
L2 (34–44) | 1 (CDR1) | 1.4 |
L3 (45–55) | 0 | |
L4 (56–79) | 1 (CDR2) | 1.5 |
L5, L6, L7, L6 (80–131) | 0 | |
L8 (132–150) | 2 | 3.0 |
L9 (151–154) | 0 | |
L10 (155–174) | 2 | 3.1 |
L11, L12, L13, L14 (175–212) | 0 | |
L15 (213–219) | 1 | 1.6 |
Antibody A, heavy chain | ||
H1, 1–43 | 0 | |
H2, 44–76 | 1 | 1.9 |
H3, 77–129 | 2 | 4.0b |
H4, H5 (130–155) | 0 | |
H6–7, 156–218 | 4 | 6.7 |
H8, H9, H10, H11 (219–230) | 0 | |
H12, H13, H14 (231–282) | 0 | |
H15, 283–296 | 2 | 2.4b |
H16–17, 297–325 | 2 | 2.9 |
H18, H19 (326–330) | 0 | |
H20, 331–334 | 1 | 1.4b |
H21, H22, H23, H24 (335–368) | 0 | |
H25, 369–378 | 1 | 1.4 |
H26, 379–400 | 3 | 4.6 |
H27, H28 (401–422) | 0 | |
H29, 423–447 | 2 | 2.8 |
H30, 448–454 | 0 |
a The amount of the substitution was estimated from peak heights of the combined mass spectra from the extracted ion chromatograms of the predicted peptide and the corresponding peptide containing the Asn → Ser substitution.
b Amounts are estimated from the endo-Asp-N peptide map of the protein (data are not shown).