Urea-Elicited Changes in Relative Electrophoretic Mobility of Certain Glycinin and β-Conglycinin Subunits
Author(s) -
Elizabeth P. B. Fontes,
M.A. Moreira,
Corinne S. Davies,
Niels Chr. Nielsen
Publication year - 1984
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.76.3.840
Subject(s) - urea , electrophoresis , sodium dodecyl sulfate , chemistry , protein subunit , biochemistry , sodium , molar ratio , polyacrylamide gel electrophoresis , gel electrophoresis , chromatography , gene , organic chemistry , enzyme , catalysis
Six molar urea in sodium dodecyl sulfate-polyacrylamide gels altered the relative electrophoretic mobility of several soybean protein subunits. Glycinin acidic polypeptide components A(3) and A(4) could be resolved from the other acidic polypeptides. A variant of the delta' subunit of beta-conglycinin was identified.
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