Importance of sodium dodecyl sulfate source to electrophoretic separations of thylakoid polypeptides.
Electrophoretic banding patterns of Chlamydomonas reinhardtii thylakoid polypeptides differ depending on whether impure, or pure sodium dodecyl sulfate (SDS) is used. Bands of Mr 45,000 and 36,000 were found when impure sodium dodecyl sulfate was used, but the Mr 45,000 band was absent when pure sodium dodecyl sulfate was used. Seven thylakoid polypeptides were isolated using preparative polyacrylamide gel electrophoresis, and the pure sodium dodecyl sulfate. Polypeptide (Mr 36,000) reran as a single band in pure sodium dodecyl sulfate, but yielded Mr 45,000 and 36,000 bands in impure sodium dodecyl sulfate. Although the Rf of most of the six other polypeptides differed, depending on whether pure or impure sodium dodecyl sulfate was used, the Mr of these polypeptides was the same with both. Thus, the banding pattern difference due to SDS source results from differences in Rf without changes in apparent Mr and a marked change in Mr of one polypeptide.
D002696:Chlamydomonas; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D012967:Sodium Dodecyl Sulfate / Q000592:standards*
D008565:Membrane Proteins; C021261:thylakoid polypeptides; D012967:Sodium Dodecyl Sulfate