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Ready identification of disulfide‐bonded polypeptides by one‐dimensional sodium dodecyl sulfate‐polyacrylamide slab gel electrophoresis
Author(s) -
Gurusinghe Asitha,
Ryan Patricia A.,
Davis Paul F.
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.1150070208
Subject(s) - sodium dodecyl sulfate , chemistry , chromatography , polyacrylamide gel electrophoresis , gel electrophoresis , gel electrophoresis of proteins , disulfide bond , sodium , polyacrylamide , electrophoresis , bovine serum albumin , alkaline lysis , albumin , alkaline phosphatase , molecular weight size marker , biochemistry , polymer chemistry , organic chemistry , enzyme , dna vaccination , gene , recombinant dna
A method for the detection of disulfide bonded polypeptide components in protein mixtures is described. During the electrophoresis of proteins in sodium dodecyl sulfate‐polyacrylamide slab gels, the migration is interrupted and advantage is taken of the rapid diffusion of added 2‐mercaptoethanol into lanes without reductant. In this paper, the results of applying this procedure to proteins known to contain only inter‐chain (α 2 ‐macroglobulin, fibrinogen, type III collagen) and intrachain disulfides (bovine serum albumin, alkaline phosphatase) as well as to crude extracts are reported.