The Effect of Variations in Ionic Strength on the Apparent Isoelectric Point of Egg Albumin
نویسنده
چکیده
The isoelectric point of ovalbumin has been determined a number of times by different methods and investigators with widely varying results (pH 4.55 to 4.88). In order to determine whether the variations of the values reported could be due to the influence exerted by the ionic strength of the buffer solvent and perhaps that of the protein itself, the writer has made a study of different concentrations of ovalbumin in several buffers of varied ionic strength.
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