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Polyacrylamide gel electrophoresis of myelin proteins: A caution

โœ Scribed by Pierre Morell; Richard C. Wiggins; Marjory Jones Gray

Publisher
Elsevier Science
Year
1975
Tongue
English
Weight
901 KB
Volume
68
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

Some variables involved in the preparation of rat brain myelin proteins for polyacrylamide gel electrophoresis in buffers containing sodium dodecyl sulfate were studied. Under mild conditions of solubilization the resultant gel patterns were relatively insensitive to the /~-mercaptoethanol (ME) concentration in the protein solvent used for solubilization of myelin proteins. However, if the samples were boiled in the presence of ME (a standard procedure for disruption of metastable aggregates of membrane proteins), a major myelin protein, proteolipid protein, as well as some minor proteins were preferentially excluded from the gel. This effect was proportional to the ME concentration.

Characterization of the polypeptide composition of membrane proteins by polyacrylamide gel electrophoresis in buffers containing sodium dodecyl sulfate (SDS) has been a standard procedure since the introduc-

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