Isotype choice for chimeric antibodies affects binding properties.
作者： M.M. Morelock , R. Rothlein , S.M. Bright , M.K. Robinson , E.T. Graham
DOI: 10.1016/S0021-9258(18)99982-5
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摘要: Abstract Construction of a series chimeric antibodies (murine variable region and human constant region) derived from the murine antibody BIRR1, which recognizes intercellular adhesion molecule 1 (ICAM-1), has revealed differences in relative binding abilities to antigen. The show ranking their ability compete with BIRR1 for antigen on surface cells order = cIgG1 (100%) > cIgG4 (30%) cIgG2 (10%) as demonstrated by solid-phase competitive enzyme-linked immunosorbent assay. Papain digestion yielded Fab fragments that were purified homogeneity. Competitive assay showed constants equivalent. A solution-phase (analyzed size exclusion high performance liquid chromatography) between intact mAbs recombinant soluble ICAM-1 further established involving arms two In summary, anti-ICAM-1 bind cellular equivalent affinities but differing avidities.
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