Glycosylation heterogeneity

Rudd PM, Dwek RA (1997), Glycosylation heterogeneity and the 3D structure of proteins, Crit. Rev. Biochem. Mol. Biol. 32 1-100. 

Kinoshita M, Mnrakami E, Oda Y, et al. (2000). Comparative stndies on the analysis of glycosylation heterogeneity of sialic acid-containing glycoproteins nsing capillary electrophoresis. J. Chromatog. A. 866 261-271. 

Characterization of C-terminal lysine variants, glycosylation heterogeneity and degradation products of recombinant antibodies demonstrates the capability of this method [60]. 

Experimentation showed that the protein was not glycosylated and that the sequence at the iV-amino acid terminus corresponded to that expected. The C-terminus sequence, however, did not correspond to that predicted and these data were interpreted in terms of the presence of a heterogeneous, truncated, protein. A study of the tryptic digest fragments from this protein with matrix-assisted laser desorption ionization (MALDI) with post-source decay enabled the authors to suggest the positions at which the parent protein had been truncated. 

Human interleukin 2, a 133-residue protein, has been separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing. Most of the heterogeneity has been attributed to variations in glycosylation of the threonine residue in position 3 of the polypep-... 

Fig. 15.7 Glycosylation of an antibody produced in tobacco plants expressing a human 3(l,4)-galactosyltransferase. As illustrated for Guy sl3 in Fig. 15.4, when the monoclonal antibody Mgr48 is produced in wild type tobacco plants (left panel), its glycosylation is structurally different and more heterogeneous than that of its mammalian counterpart (lower panel). When this antibody is produced in tobacco plants expressing the human galactosyltransferase (right panel), 30% of its N-glycans show terminal N-acetyllactosamine sequences identical to those carried by this antibody when it is produced in hybridoma cells.

Apart from the heterogeneity of apo(a), caused by a varying number of Lpa-KIV2-kringles and the degree of glycosylation (varying up to 35%) (G26), human Lp(a) seems to exist of two species with different affinities for lysine-Sepharose (L13), but similar interaction with LDL-receptor in vitro (A15). This... 

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