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Analysis of members of the Ig‐gene superfamily by thermal gradient polyacrylamide gel electrophoresis
Author(s) -
Tulp Abraham,
Verwoerd Desireé
Publication year - 1992
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.11501301139
Subject(s) - monomer , polyacrylamide gel electrophoresis , electrophoresis , chemistry , gel electrophoresis , polyacrylamide , chromatography , thermal stability , peptide , polymer , biochemistry , polymer chemistry , organic chemistry , enzyme
A solid aluminum block, connected with a warm and cold thermostated waterbath, provided for a linear transversal temperature gradient (TG) during polyacrylamide gel electrophoresis (PAGE). Noncovalently bound heavy chain dimers as well as heavy‐light chain dimers, derived from human monoclonal IgG, could be melted into monomers using a 40–75°C TG under conditions of sodium dodecylsulfate‐PAGE. Using native PAGE, majorhistocompatibility complex (MHC) class I molecules, preloaded with the iodinated peptide FAPGNYPAL could be melted in a 4–40°C TG to release the peptide. The method is in general applicable to thermal stability analysis of noncovalently bound hetero‐oligomers if the product after melting possess different electrophoretic mobilities.