Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults

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Abstract
A method of zone electrophoresis in which starch gel is used as the supporting medium is described. Protein detection is by staining. The resolving power is in many cases superior to that obtained by the Tiselius method. As little as 0.02 ml of sample can be used, if necessary, and the method is very well adapted to comparing closely related samples. When the method is used for the electrophoresis of normal human sera several previously undescribed non-dialyzable components may be demonstrated. These components can be seen with several buffers, including barbiturate. A borate buffer is normally employed. The period of electrophoresis is 16 hours. Electrophoretic anomalies, products of the clotting process, and inadvertent hemolysis as sources of the new components are excluded. Sera from over 40 normal human adults of both sexes are found to fall into 3 groups on the basis of the occurrence of some of the new components. No difference in the distribution of the groups in the sexes was shown. The components characterizing the 3 groups have a common property, not shared by any other of the serum proteins, of binding hemoglobin under the conditions used for electrophoresis. They migrate in the a2-globulin position when filter-paper electrophoresis is used. The occurrence of the characteristic proteins may be related to age and to hereditary factors. Possible reasons for the high resolving power of the new method and its limitations are discussed.

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