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Applicability of the log MM ‐ √D relationship to linear polyacrylamide gradient gel electrophoresis under a wide range of experimental conditions
Author(s) -
Rothe G. M.
Publication year - 1982
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150030504
Subject(s) - linearity , logarithm , electrophoresis , analytical chemistry (journal) , chromatography , gel electrophoresis , chemistry , linear regression , linear relationship , immobilized ph gradient , capillary electrophoresis , linear correlation , mathematics , isoelectric focusing , physics , mathematical analysis , statistics , biochemistry , quantum mechanics , enzyme
Recently we reported about a linear correlation between the logarithm of the size of native proteins (log mol mass or log Stokes' radius) and the square root of their migration distance (‐ √D) in linear polyacrylamide (PAA)‐gradient gels (G. M. Rothe and H. Purkhanbaba, Electrophoresis 1982, 3 , 33–42). The linearity between log MM and √D is not subject to time using homogeneous buffers in electrophoresis, no matter how the constants of the corresponding regression lines, slope and intercept change as a function of time. The realiability of this correlction has been re‐examined with 0.7 mm thin gel plates and extending the time of electrophoresis under non‐denaturating conditions from 2 to 95 h. It is demonstrated that the linear log size ‐ √D‐relationship is also applicable to sodium dodecyl sulfate (SDS) linear PAA gradient gel electrophoresis.