Abstract
The C.D. spectra of two IgD myeloma proteins and their enzymatically derived Fab δ and Fc χ fragments have been studied. The intact proteins differ from each other in the presence of a strong positive band at 235 nm, present in one protein only. The structural feature responsible for this difference is clearly demonstrated to be localized within the Fab δ region. No significant conformational change is detected on proteolytic cleavage since the sum of the contrbiutions of the fragments is equivalent to the intact protein.
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