Electrophoretic experiments of red blood cell hemolysates obtained by hemolysing with distilled water were carried out, in order to prove the allergic antibody, which has geen expected to adhere in the erythrocyte. Results obtained are as follows.
1). The electrophoretic patterns were obtained on 9 rabbit, 28 human, and 2 goat red blood cell hemolysates from which stroma were removed. In these diagrams there were recorded a, c, Hb and b components mobilities of which were about -4.3, -1.9, and -1.1×10
-5cm. 2 per volt per second at pH 8.0, respectively.
2). b protein in rabbit and c protein in human red blood cell hemolysates were hardly demonstrable, but c protein in goat was remarkable.
3). In rabbit red blood cell hemolysates, which were sensitized with the mixture of phosphatides of rabbit erythrocytes and ox sera or with ox sera only, the peak which was thought to be allergic antibody (X protein) was recorded as a component having mobility faster than Hb protein. The mobility of this pritein is about -2.9×10
-5cm. 2 per volt per second. This peak disappeared at the 2nd day after reinjection of the antigen mentioned above.
4). Some of human erythrocytes, in septicemia, subacute bacterial endocarditis and rheumatic diseases had X peak. In the bone marrows of these patients the erythropoesis was almost attacked. Not all the anemic diseases had X peak in toeir eryterocytes.
5). c protein seems to be rich in lipid on account of its decrease of the area of electrophoretic pattern after extraction. It is interesting to find that in two cases of nephritic human cryrocytes, c component was remarkable.
6). It is doubtful whether the peak appearing before or bshind Hb perk is due to the denaturing product either in vivo or in vitro, but it is more enhanced in rhcumatic diseases.
In summer Hb peak were divided clearly into two peaks by denaturation when red blood cell hemolysates were kept at room temperature.
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