ABSTRACT
The production and clinical applications of human recombinant glycoproteins for therapeutic administration have been an area of intensive scientific and medical efforts. The successful introduction in human therapy of recombinant proteins such as insulin, growth hormone, and α-interferon led many pharmaceutical companies to extend the production of recombinant proteins to the numerous compounds. Only in recent years has the functional importance of glycans to in vivo efficiency of recombinant glycoproteins become widely recognized, and it is clear that the glycosylation of recombinant proteins can affect their pharmacokinetics, biodistribution, and immunogenicity. It is interesting to note that cell transfection with deoxyribonucleic acid can activate latent glycosyltransferases. Glycosylation has the potential to affect the level of expression; physicochemical, pharmacokinetic, and immunological properties; biological activity; clinical efficacy; and stability of recombinant glycoproteins. Consequently, decreased glycosylation or sialylation could affect the solubility of a glycoprotein, leading to low recoveries during isolation and purification and to increased formation of aggregates.
