Glycosylation of therapeutic proteins: Current understanding of structure-function relationships

BioProcess International

Volumn 9, Issue 6, 2011, Pages 48-53

  Siemiatkoski, Joseph ^a   Ma, Stacey ^b   Park, Jun ^c   Brorson, Kurt ^c   Swann, Patrick ^c   McLeod, Lorna ^d  

^a Percivia LLC   (United States)

^b GENENTECH INC   (United States)

^c CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^d NONE

Author keywords

Analytical methods; Carbohydrates; Characterization; Lot release; MAbs; Stability

Indexed keywords

CAPILLARY ELECTROPHORESIS; ELECTROSPRAY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE IMAGING; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; SHORT SURVEY; STRUCTURE ACTIVITY RELATION;

EID: 80052348042     PISSN: 15426319     EISSN: None     Source Type: Trade Journal    
DOI: None     Document Type: Short Survey

References (3)

1. Shields RL, et al. Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-Dependent Cellular Toxicity. J. Biol. Chem. 277, 2002: 26733-26740.
2. Kaneko Y, Nimmerjahn F, Ravetch J. Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation. Science 313, 2006: 670-673.
3. Jones AJS, et al. Selective Clearance of Glycoforms of a Complex Glycoprotein Pharmaceutical Caused By Terminal N-Acetylglucosamine Is Similar in Humans and Cynomolgus Monkeys. Glycobiol. 17, 2007: 529-540.