The Electrophoretic Properties of Serum Proteins
نویسندگان
چکیده
Numerous investigations have been carried out during the past decades dealing with the preparation and properties of crystalline horse serum albumin. While several modifications of the classical methods and conditions for the crystallization of this protein and its components have been introduced in recent years (l-6), the electrophoretic properties of any one fraction have not yet been investigated over a wide pH range with the refined optical methods for recording boundary shape. Although the electrophoretic mobility of horse serum albumin has been determined at pH regions other than that of the physiological range of about 7.6, a detailed resolution of the boundaries into their component parts was not possible with the experimental methods that were employed (2, 7-9). The present paper describes an electrophoretic analysis of fractions of crystalline serum albumin, preps& according to Kekwick (2), carried out kvith the: Tisclius clectrophoresis apparatus in conjunction with the Thoevert-Philpot-Svensson optical system. Boundary anomalies seen in slightly acidified solutions of these proteins prompted measurements on a number of other preparations obtained by the methods of crystallization summarized in a recent publication from this laboratory (5). Comparative measurements on native protein and on the same material after apparent reversal of denaturation by concentrated urea solutions (9) are also recorded in this paper.
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تاریخ انتشار 2003