Photometric Microdetermination of Human Gamma
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چکیده
The main purpose in performing the detailed experimental studies in Part I is the application of the photometric method to the determination of the gamma globulin content of human sera. These experimental studies show that protein fractions such as albumin or alpha globulins, whose electrophoretic mobilities are far removed from gamma globulin, cause little interference with its determination. Whereas those fractions, such as beta globulins or fibrinogen, whose electrophoretic mobilities are close to that of gamma globulin, are apt to cause positive errors, unless their concentrations are reduced below a certain critical ratio, as compared to gamma globulin. This furnishes experimental evidence that there is a relationship between mobility and flocculation of protein fractions which is to be expected from theoretical considerations (1). A similar close parallelism between mobility and solubility of proteins in concentrated salt solution, e.g., ammonium sulfate, has been pointed out by Svensson (2) and Pedersen (3). Svensson concludes that it is not a simple matter to isolate pure electrophoretic components by salt fractionation. His results were confirmed by the careful experimental studies of Majoor (4) on the solubility of protein fractions in various concentrations of sodium sulfate in comparison with results of electrophoresis experiments. His results show that particularly in the case of disease sera, a wide range of concentrations of sodium sulfate is required for complete precipitation of gamma globulin. He states that at any single salt concentration there is undeniable overlapping of protein fractions and no absolute separation takes place. The experimental technique in this paper conforms closely
منابع مشابه
Photometric microdetermination of human gamma globulin. I. Development of a quantitative flocculation-ninhydrin procedure.
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تاریخ انتشار 2013