pubmed-article:18201853 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:18201853 | lifeskim:mentions | umls-concept:C0667569 | lld:lifeskim |
pubmed-article:18201853 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:18201853 | pubmed:dateCreated | 2008-4-11 | lld:pubmed |
pubmed-article:18201853 | pubmed:abstractText | Two degradations of aspartate residues located in Asp-Asp motifs in the CDR3 region of a recombinant monoclonal antibody were identified and quantified after the antibody was aged in a mildly acidic buffer at elevated temperatures. The degraded sample aged at 25 degrees C for 1 month generated 1.8% antibody molecules that had isomerization in the aspartate residues, while the degraded sample after aging at 45 degrees C for 1 month contained 7% isomerization. Peptide bond cleavages at the aspartate residues were also detected and characterized. The percentage of clipped antibody molecules after 1 month of storage was 1% at 25 degrees C and 4.4% at 45 degrees C. The generated cleaved polypeptides were noncovalently attached to the intact antibody molecule and were not involved in the aggregation formation. They were not detected by native size-exclusion chromatography because of their strong non-covalent association to the rest of the antibody molecules. On the other hand, the cleaved polypeptides were dissociated and detected as fragments under denaturing conditions of reversed-phase HPLC, denaturing size-exclusion chromatography and MALDI-TOF mass spectrometry. It was demonstrated that the cleavages at the above aspartate residue sites occurred due to the aging of the sample at elevated temperatures and were not method-induced by the reversed-phase HPLC and other methods used in this study. | lld:pubmed |
pubmed-article:18201853 | pubmed:language | eng | lld:pubmed |
pubmed-article:18201853 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18201853 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18201853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18201853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18201853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18201853 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18201853 | pubmed:month | May | lld:pubmed |
pubmed-article:18201853 | pubmed:issn | 0731-7085 | lld:pubmed |
pubmed-article:18201853 | pubmed:author | pubmed-author:BondarenkoPav... | lld:pubmed |
pubmed-article:18201853 | pubmed:author | pubmed-author:XiaoGangG | lld:pubmed |
pubmed-article:18201853 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18201853 | pubmed:day | 12 | lld:pubmed |
pubmed-article:18201853 | pubmed:volume | 47 | lld:pubmed |
pubmed-article:18201853 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18201853 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18201853 | pubmed:pagination | 23-30 | lld:pubmed |
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pubmed-article:18201853 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18201853 | pubmed:articleTitle | Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody. | lld:pubmed |
pubmed-article:18201853 | pubmed:affiliation | Amgen, Department of Pharmaceutics, One Amgen Center Drive, Thousand Oaks, CA 91320, USA. | lld:pubmed |
pubmed-article:18201853 | pubmed:publicationType | Journal Article | lld:pubmed |