EPITOPE CHARACTERIZATION OF MUC1 ANTIBODIES

Citation
S. Imai et al., EPITOPE CHARACTERIZATION OF MUC1 ANTIBODIES, Tumor biology, 19, 1998, pp. 30-34
Citations number
11
Categorie Soggetti
Oncology
Journal title
ISSN journal
10104283
Volume
19
Year of publication
1998
Supplement
1
Pages
30 - 34
Database
ISI
SICI code
1010-4283(1998)19:<30:ECOMA>2.0.ZU;2-X
Abstract
The 56 MAbs submitted to the ISOBM TD-4 Workshop were analysed by ELIS A assay for reactivity against synthetic MUC1 mucin protein core-relat ed peptides. With peptides comprising 5, 7 and 20 amino acids, 4/56 (7 .1%), 33/56 (58.9%) and 51/56 (91.1%) of antibodies showed positive re activity, respectively, Peptides with 60, 80, 100 and 120 amino acids showed 50/56 (98.2%), 54/56 (96.4%), 53/56 (94.6%) and 47/56 (83.9%) a ntibodies with positive reactivity, respectively. The reactivity of ea ch MAb with synthetic peptides was classified into 3 groups. In group A(15 MAbs), the reactivity increased depending on the peptides in leng th and was maximal with 20-, 60-, 80-, 100- and 120-mer peptides. In g roup B (24 MAbs), most antibodies showed very weak binding affinity to peptides with a small increase in reactivity with the 100- and 120-me r peptides. In group C (17 MAbs), the reactivity showed strong binding affinity with the 20-mer peptide followed by a reduced uneven pattern of reactivity with the 60-, 80-, 100- and 120-mer peptides. These res ults show that the binding affinity of MAbs against synthetic peptides does not depend on the recognition of antibodies to the epitopes of c ore protein.