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Toward a steady‐state pore limit electrophoresis dimension for native proteins in two‐dimensional polyacrylamide gel electrophoresis
Author(s) -
Fawcett John S.,
Sullivan James V.,
Chrambach Andreas
Publication year - 1989
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.1150100305
Subject(s) - polyacrylamide gel electrophoresis , electrophoresis , polyacrylamide , gel electrophoresis of proteins , gel electrophoresis , chemistry , chromatography , two dimensional gel electrophoresis , redistribution (election) , biochemistry , polymer chemistry , enzyme , proteomics , gene , politics , political science , law
Polyacrylamide gel electrophoresis in linear pore gradients (4.8 to 48 %T, 5 %C Bis ) provides for migration arrest, in a practical sense, after about 5000 Vh for proteins of 290 and 450 kDa, but not for smaller proteins over 20 000 Vh. The arrest is not due to inadequate field strength nor is it caused by water redistribution within pore gradien gels. The possibility is being discussed that exponential pore gradients, and a higher or a lower degree of crosslinking suggested by the literature may be remedies for the present failure to arrest the migration of smaller proteins.