Abstract
Monoclonal IgG belonging to the different rat IgG subclasses and IgG2a from normal rat serum were subjected to enzymatic degradation with papain and pepsin under several experimental conditions. IgG1 was found the most resistant to papain and IgG2a the most sensitive when the proteins were incubated in absence of cysteine or with low concentrations of the reducing agent (0.001 M). Papain digestion in the presence of 0.01 M cysteine led to the release of non-covalent Fc from rat IgG1, IgG2a and IgG2b. IgG1 and IgG2a were the most resistant to pepsin degradation, whereas IgG2c had very high sensitivity to the action of this enzyme. The effects of the increase of pepsin concentration and of the addition of cysteine were found to be different according to the IgG subclass. The pepsin Fc (pFc) fragment was generated in significant yields from rat IgG2a and IgG2c, but was absent from pepsin digests of IgG1. The mechanisms of resistance to proteolysis and its possible biological significance have been discussed.
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