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Influence of the state of denaturation on the migration of adenovirus type 2 structural proteins in sodium dodecyl sulfate polyacrylamide gels
Author(s) -
CailletBoudin Marie L.,
Lemay Pierre
Publication year - 1986
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.1150070705
Subject(s) - sodium dodecyl sulfate , denaturation (fissile materials) , polyacrylamide , chemistry , urea , polyacrylamide gel electrophoresis , sodium , chromatography , disulfide bond , biophysics , guanidine , electrophoresis , biochemistry , polymer chemistry , organic chemistry , nuclear chemistry , biology , enzyme
The changes in the migration of adenovirus type 2 structural proteins in sodium dodecyl sulfate polyacrylamide gels following various denaturation conditions or periods have been studied. Several factors such as proteolytic cleavages, disulfide bridges, carbamylation or residual charge effects which could lead to altered migration were screened. Resistant high order structures sensitive to the action of urea might cause these variations. A likely relationship between the difference of apparent molecular weight, frictional coefficient and hydrophobicity has been established.