On the Migration Distance of Amino Acids and Serum Proteins in Paper-electrophoresis Part. IV

Peviously we reported on the migration distance and newly defined MG values of amino acids in paper-electrophoresis and pointed out that the MG of amino acids in our definition-the distance ratio of amino acids from glycine to that of aspartic acid-changed their own values as the function of pH of surrounding buffer solution. These results suggested that in paper-electrophoresis the mobilities of amino acids were the function of pH of buffer. Kunkel and Tiselius decided the mobilities of serum proteins by measuring the distance of migrants from dextran as the net migration distance, clamping paper strips between glass plates to exclude the effect of electro-osmotic flow and evaporation of buffer from paper surface. In the present paper a description is given of measuring the net migration distance by the above method, in which disturbing factors such as evaporation, heating and buffer concentration gradient were reduced to minimum, and of applying the MG values to serum proteins. An attempt was made to determine the apparent migration distance from original point, the distance of static point of migrant from origin and the initial velocity of migration by the experimental formulas obtained in the common apparatus, in which the evaporation from filterpaper was admitted