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Determination of molecular weights and stokes radii of nondenatured proteins by poly acrylamide gradient gel electrophoresis 2. determination of the size of stable and labile molecular weight variants of enzymes from plant sources



Determination of molecular weights and stokes radii of nondenatured proteins by poly acrylamide gradient gel electrophoresis 2. determination of the size of stable and labile molecular weight variants of enzymes from plant sources



Electrophoresis 3(1): 43-48



Under certain conditions in polyacrylamide gradient gel electrophoresis (PAGGE), a linear correlation between the logarithm of the size of calibration proteins (log MW or log RS [stokes' radius]) and the square root of their migration distance .**GRAPHIC**. can be observed; slope and intercept of the calibration curve depend on the duration of electrophoresis; linearity, however, is maintained over a wide range (4-60 h, 200 V). Using this method the reaction of plant isozyme systems penetrating a linear polyacrylamide (PAA) gradient gel was investigated: lactate dehydrogenase (LDH) [EC 1.1.1.27] from potato tubers behaves similarly to animal calibration proteins. The enzyme exhibits 3 subbands with MW of 144,000, 150,000 and 156,000 (.+-. 1.7%), respectively. The [pea] enzyme system shikimate oxidoreductase (SORase) [EC 1.1.1.25] behaves significantly different: during PAGGE it splits into 2 major bands (.apprx. 60,000 and .apprx. 110,000, respectively) consisting of several subbands. SORase is present in vivo as a complex system. This complex may be partly identical with the so-called pre-chorismate complex.

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