PMID: 9422094Jan 9, 1998Paper

Effect of desialylation on binding, affinity, and specificity of 56 monoclonal antibodies against MUC1 mucin

Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine
J DaiK K Yeung

Abstract

We evaluated 56 monoclonal antibodies (MAbs), submitted to the ISOBM TD-4 Workshop, for changes in binding following desialylation of the MUC1 molecule and for epitope specificity. Antibody binding of MAbs was assayed by an ELISA method using microtiter plates coated with the MUC1 mucin obtained from supernatants of the ZR75-1 cell line. The MUC1 mucin was desialylated directly on the plate by treatment with neuraminidase. For each MAb, binding to untreated mucin was compared over a range of antibody concentrations. The concentration at which binding was half-maximal (K50) was determined for all antibodies whose binding reached saturation in the assay. Results showed that K50 values for MAb binding to untreated MUC1 mucin varied from 10(-10) to 10(-6) M. These data suggest that MAbs to MUC1 mucin bind with a broad range of intrinsic affinities. Desialylation was found to have variable effects on antibody binding, in that binding was either increased, decreased, or unchanged. No relationship was found between the apparent affinities for untreated mucin and changes in binding following desialylation. Among the 56 Workshop MAbs, 33 were found reactive with synthetic peptides which mimic the MUC1 tandem repeat. We determined the ep...Continue Reading

Citations

Feb 13, 2002·Hybridoma and Hybridomics·W QiR Madiyalakan
Feb 9, 2005·DNA and Cell Biology·Yue-Jin WenThomas Kieber-Emmons
Feb 21, 2006·Biochemistry. Biokhimii︠a︡·S J Golubović, Z T Bojić-Trbojević
Sep 11, 2003·Clinical Chemistry and Laboratory Medicine : CCLM·Petr SternVladimir Palicka
Nov 11, 2009·Journal of the American Chemical Society·Naoki OhyabuShin-ichiro Nishimura

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