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[Immunochemical and biological properties of rapid monoclonal proteins of the IgG class]
Four proteins M class IgG were analysed in detail in view of their more rapid electrophoretic migration in starch gel among most proteins in this class. On the basis of these investigations two protein (from sera 212 and 244) corresponded to subclass IgG-4, one (serum 119) probably to IgG-4 with polyclonal impurities from other subclasses, and the fourth protein (from serum 210) to subclass 3 or 1. Since subclass IgG-4 contains the greatest amount of sialic acid residues of the remaining IgG subclasses finding of more rapid migration of the observed proteins seems to be due to this. A hypothesis has been put forward that if rapidly moving IgG do not belong to subclass 4 then they have, probably, atypically arranged carbohydrate groups, e.g. in Fab fragment. It was found also that the studied proteins M were carried during chromatography with DEAE cellulose only when a buffer with higher concentration of NaCl was used.
Four proteins M class IgG were analysed in detail in view of their more rapid electrophoretic migration in starch gel among most proteins in this class. On the basis of these investigations two protein (from sera 212 and 244) corresponded to subclass IgG-4, one (serum 119) probably to IgG-4 with polyclonal impurities from other subclasses, and the fourth protein (from serum 210) to subclass 3 or 1. Since subclass IgG-4 contains the greatest amount of sialic acid residues of the remaining IgG subclasses finding of more rapid migration of the observed proteins seems to be due to this. A hypothesis has been put forward that if rapidly moving IgG do not belong to subclass 4 then they have, probably, atypically arranged carbohydrate groups, e.g. in Fab fragment. It was found also that the studied proteins M were carried during chromatography with DEAE cellulose only when a buffer with higher concentration of NaCl was used.