Abstract
The catabolism of myeloma proteins of the γG-subclasses γG1 and γG2 were measured in a healthy volunteer and contrasted with that of γG-globulin preparations containing all four subclasses and isolated from various sources.
The γG2 protein had a biological half-life of 24 days, showing no evidence of catabolic heterogeneity as measured over a period of 7 weeks. In contrast, the γG1 protein showed some catabolic heterogeneity, the half-life increasing from 15 to 19 days over the same period. It is possible that molecules of γG1-globulins may exist in different conformational forms.
The catabolism of whole γG-globulin is heterogeneous. This can be substantially explained in terms of the resultant catabolic pattern of mixtures of γG1- and γG2-globulin molecules.
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Selected References
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