1 Background N-glycosylations affect important properties such as the specificity, efficacy, immunogenicity and stability of proteins. A portfolio of methods for glycan analysis was developed, using the murine monoclonal antibody 1RK1, an IgG1κ, to enable N-glycosylations of proteins to be analysed (Fig. 1). The methods developed were subsequently applied to the plant glycoprotein ricin.
Glycosylations should not be neglected for the correct calculation of the molecular mass, the isoelectric point and the mass-specific UV absorption coefficient. Therefore Prot pi provides a tool to draw glycans as a posttranslational modification of proteins. This short guide deals with how to add two complex-type N-Glycosylation G1 with a sialic acid (N-acetylneuraminic acid) […]