作者: M. STEINBUCH , C. REUGE , R. AUDRAN , A. FAURE , M.M. ZAKIN
DOI: 10.1016/B978-0-08-013348-5.50033-8
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摘要: Summary The biological activities of immunoglobulins are not affected equally by chemical modifications. sites IgG responsible for the fixation complement and interaction with rheumatoid factor seem to be more labile than those concerned antibody activity. destruction Try Met causes a drastic modification both IgA, latter being even somewhat labile. present study confirmed earlier results showing that there is always parallelism between amount aggregated material anticomplementary activity in IgG. Certain chemically modified preparations having lost their become again after heating this can also found digestion papain certain Fc-fragments. However, other substituted molecules definitely devoid