Abstract：
:Measurement of the total target ligand can help to provide pharmacokinetic (PK) and pharmacodynamic (PD) informations. However, the presence of monocloncal antibody therapeutics (ThAs) interferes with ELISA determinations of the total target proteins. The interferences can cause over- or under-estimation of the target protein analysis. The nature of interferences was dependent upon the ThA, target protein, antibody reagents and assay conditions of the ELISA. We have developed novel alkaline and acid/guanidine treatment approaches to dissociate the protein binding and preferentially denature the ThA. The neutralized target proteins can be determined by ELISA. These methods provide reproducible measurements of total target protein without ThA interference. Serum samples, standards and QCs containing target protein and ThA were treated with alkaline buffer (pH>13) containing casein or acid/guanidine buffer (pH<1). Total target proteins for two different ThA systems were successfully measured and interferences were completely eliminated by the treatments. These methods were successfully applied to analysis in pre-clinical serum samples.
journal_name
J Pharm Biomed Analjournal_title
Journal of pharmaceutical and biomedical analysisauthors
Salimi-Moosavi H,Lee J,Desilva B,Doellgast Gdoi
10.1016/j.jpba.2009.11.021subject
Has Abstractpub_date
2010-04-06 00:00:00pages
1128-33issue
5eissn
0731-7085issn
1873-264Xpii
S0731-7085(09)00717-1journal_volume
51pub_type
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