Document Detail


Fractionation of follicle stimulating hormone charge isoforms in their native form by preparative electrophoresis technology.
MedLine Citation:
PMID:  16198015     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Complex glycoprotein biopharmaceuticals, such as follicle stimulating hormone (FSH), erythropoietin and tissue plasminogen activator consist of a range of charge isoforms due to the extent of sialic acid capping of the glycoprotein glycans. Sialic acid occupies the terminal position on the oligosaccharide chain, masking the penultimate sugar residue, galactose from recognition and uptake by the hepatocyte asialoglycoprotein receptor. It is therefore well established that the more acidic charge isoforms of glycoprotein biopharmaceuticals have higher in vivo potencies than those of less acidic isoforms due to their longer serum half-life. Current strategies for manipulating glycoprotein charge isoform profile involve cell engineering or altering bioprocesss parameters to optimise expression of more acidic or basic isoforms, rather than downstream separation of isoforms. A method for the purification of a discrete range of bioactive recombinant human FSH (rhFSH) charge isoforms based on Gradiflowtrade mark preparative electrophoresis technology is described. Gradiflowtrade mark electrophoresis is scaleable, and incorporation into glycoprotein biopharmaceutical production bioprocesses as a potential final step facilitates the production of biopharmaceutical preparations of improved in vivo potency.
Authors:
Dallia Catzel; David Y Chin; Peter G Stanton; Peter P Gray; Stephen M Mahler
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Publication Detail:
Type:  Journal Article     Date:  2005-09-27
Journal Detail:
Title:  Journal of biotechnology     Volume:  122     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-22     Completed Date:  2006-04-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  73-85     Citation Subset:  IM    
Affiliation:
Bioengineering Centre, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, Australia.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biotechnology / methods*
CHO Cells
Chemical Fractionation / methods*
Cricetinae
Cricetulus
Electrophoresis / methods*
Follicle Stimulating Hormone / genetics,  isolation & purification*
Humans
Protein Engineering / methods*
Protein Isoforms / genetics,  isolation & purification
Chemical
Reg. No./Substance:
0/Protein Isoforms; 9002-68-0/Follicle Stimulating Hormone

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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