Glycosylation is a non-template-driven posttranslational modification during which linked-sugars and glycans are added to the nascent polypeptide. Over 70% of the eukaryotic proteome is thought to be glycosylated. It is now known that correct glycosylation is essential for the correct folding, solubility, stability, and immunogenicity of proteins.
View Article and Find Full Text PDFHydroxyapatite (HA) is a mixed-mode media that has been used extensively for the purification of proteins and DNA since the 1950s. Hydroxyapatite possesses a distinctive selectivity that may be applied in the purification of a wide range of biomolecules: immunoglobulins, alkaline proteins, acidic proteins, and DNA. The functional groups of HA can both attract and repel the carboxyl and amino groups on target molecules.
View Article and Find Full Text PDFMany proteins are glycosylated, that is to say they have bound sugars or glycans. Glycosylation is a non-template-driven posttranslation modification. It is now known that correct glycosylation is essential for the correct folding, solubility, stability, and immunogenicity of proteins.
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