Papain susceptibility and optical rotatory dispersion of reassociated autologous H and L chains of monotypic IgG2 and IgG4 proteins

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Abstract

The ORD (optical rotatory dispersion) and papain digestibility of papain resistant IgG2 and IgG4 myeloma proteins and of their reassociated autologous alkylated or nonalkylated H and L chains were investigated. The Moffitt constants of the native proteins and of the reassociated chains were found to be near zero. The papain digestibilities of reassociated non alkylated chains and alkylated chains proved to be different. Susceptibility to papain is therefore a sensitive indicator of conformation changes of IgG molecules even if the ORD values do not show any differences.

Original languageEnglish
Pages (from-to)303-308
Number of pages6
JournalActa Biochimica et Biophysica Academiae Scientiarum Hungaricae
Volume9
Issue number4
Publication statusPublished - Dec 1 1974

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ASJC Scopus subject areas

  • Medicine(all)

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