Linked Life Data

16375256

Source:http://linkedlifedata.com/resource/pubmed/id/16375256

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-12-26
pubmed:abstractText
Structural heterogeneity of recombinant IgG1 antibodies derives from variations in conserved as well as unique structural features. Common sources of heterogeneity include Fc glycosylation, partial heavy chain C-terminal Lys processing, Fc methionine oxidation, hinge-region cleavage, and the glycation of Lys residues. Aspartate residues that are isomerized to iso-aspartate were detected by cation exchange or hydrophobic interaction chromatography for trastuzumab and omalizumab, respectively. Unpaired cysteines were detected in omalizumab using Ellman's reagent, with the thiol-containing Fab resolved using hydrophobic interaction chromatography after papain digestion. Structural variations that cause chromatographic resolution may indicate the presence of a form with reduced potency.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1424-6074
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
117-27
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Heterogeneity of recombinant antibodies: linking structure to function.
pubmed:affiliation
Analytical Chemistry Department, Genentech, Inc, South San Francisco, CA 94080, USA. reed@gene.com
pubmed:publicationType
Journal Article