Abstract
The detailed characterization of complex protein mixtures like samples from biological sources cannot be sufficiently performed by separation of polypeptides accordingly to their molecular weight as is done by conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (1DE). For analysis of such samples, two-dimensional gel electrophoresis (2DE) is the preferable methodological approach, since it combines separation of polypeptides according to isoelectric properties and molecular weight as well. The resulting pattern of protein spots does not only provide information on composition of samples due to the complexity of a mixture of polypeptides. It delivers also a picture on the microheterogenity of polypeptides caused by posttranslational modifications. These might be of natural or artificial type and occur during biosynthetic processing of a polypeptide or within industrial scale production.
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© 2002 Humana Press Inc.
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Löster, K., Kannicht, C. (2002). 2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern . In: Kannicht, C. (eds) Posttranslational Modifications of Proteins. Methods in Molecular Biology™, vol 194. Humana Press. https://doi.org/10.1385/1-59259-181-7:301
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DOI: https://doi.org/10.1385/1-59259-181-7:301
Publisher Name: Humana Press
Print ISBN: 978-0-89603-678-9
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