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Determination of molecular weights and stokes radii of nondenatured proteins by polyacrylamide gradient gel electrophoresis 3. estimation of the upper and lower size limits of carbonic anhydrase ec 4.2.1.1 as a model for complexing enzymes



Determination of molecular weights and stokes radii of nondenatured proteins by polyacrylamide gradient gel electrophoresis 3. estimation of the upper and lower size limits of carbonic anhydrase ec 4.2.1.1 as a model for complexing enzymes



Electrophoresis 6(4): 147-154



Studying the separation behavior of various native carbonic anhydrase isozymes from mammalian erythrocytes showed that the migration of these enzymes differs from that of the marker proteins commonly used in gradient gel electrophoresis. In alkaline buffer systems the enzymes from human, bovine, rabbit, and canine erythrocytes start to migrate with a size apparently 6 to 12 times larger than their monomeric size, then gradually lose in apparent size and finally end up in a size equivalent to their monomeric molecular mass. The monomeric molecular mass of the various carbonic anhydrase forms were determined to be 23,000-39,000 (g/mol). These values are in accordance with different data in the literature and the data which we obtained by sodium dodecyl sulfate-gradient gel electrophoresis. The equations and the graphical solutions needed to calculate the apparent upper size as well as the monomeric size of mammalian carbonic anhydrases are presented. Only the time-dependent version of non-enaturing poly-acrylamide gradient gel electrophoresis provides reliable molecular mass estimations.

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