Abstract
Human γ globulins are shown by means of special antisera and papain digestion to consist of three to five different species which share only some of their determinants. A minimum total number of eight determinants is suggested. Only four of these determinants are possessed by the bulk of the serum globulins and one of these four determinants is shown to be shared with the cryoglobulin of a Waldenström serum. This cryoglobulin is shown to have a further minimum of two determinants shared with one of the subsidiary γ globulins occurring in normal human sera, as well as at least one specific determinant not found in normal sera. Other macroglobulinaemic sera are shown to have variable amounts of globulins antigenically related to this cryoglobulin and even normal sera appear to have traces of such macroglobulins. All γ globulins appear to be split more readily than other serum proteins, but the Waldenström macroglobulin more readily still. It is suggested that the slight forking of the γ-globulin line often seen in immuno-electrophoretic patterns near the cathode side may be due to the existence of antigenically related, but not identical, γ globulins whose range of electrophoretic mobilities does not quite overlap there and may vary in different subjects. The previously suggested spontaneous or enzymatic cleavage remains another possible explanation.
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