Monoclonal antibodies to bovine serum albumin: Affinity and specificity determinations

Guillemette A. Morel, David M. Yarmush, Clark K. Colton, David C. Benjamin, Martin L. Yarmush

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

A panel of 12 monoclonal antibodies (MAb) to bovine serum albumin (BSA) was developed and characterized as to their physicochemical and immunological properties. Affinity constants of the MAb varied over a wide range from 105 to 108 M-1. MAb were assembled into several groups of non- or minimally interacting antibodies by analysis of competitive binding experiments, and BSA domain and subdomain specificities of the MAb were assigned by analysis of results of MAb binding to purified BSA fragments. Further fine specificity delineation was accomplished by examination of cross-reactivity patterns to several mammalian albumins. The data suggest that some of the low affinity MAb recognize sites on different portions of the BSA molecule, indicating that similar epitopes exist on different domains of the BSA molecule.

Original languageEnglish (US)
Pages (from-to)7-15
Number of pages9
JournalMolecular Immunology
Volume25
Issue number1
DOIs
StatePublished - Jan 1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

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