Analysis of glycoforms on the glycosylation site and the glycans in monoclonal antibody biopharmaceuticals

Ucakturk E.

JOURNAL OF SEPARATION SCIENCE, vol.35, no.3, pp.341-350, 2012 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Review
  • Volume: 35 Issue: 3
  • Publication Date: 2012
  • Doi Number: 10.1002/jssc.201100684
  • Page Numbers: pp.341-350


Therapeutic monoclonal antibodies (mAbs), immunoglobulins, have been efficiently used in the treatment of many diseases, such as cancer, inflammatory and cardiovascular diseases, and organ transplantation. mAbs are glycoprotein molecules undergoing posttranslational modifications. Glycosylation is one of the posttranslational modifications. Different glycoforms that are important for maintaining the potency of mAb drugs show various biological activities. Therefore, the profile of the glycans and glycosylation sites should be determined to produce safe, good quality, consistent mAb drugs for human use. For this reason, simple, robust, accurate, and reproducible analytical methods need to be developed. In this article, chromatographic methods for the analysis of the glycoforms on the glycosylation site and the glycans in mAb biopharmaceuticals have been evaluated.