Abstract

Poster Presentations

Day 1, May 17（Wed.）　　Room P (Multi-purpose Hall)

1P-55　　PDF

Bioanalysis of therapeutic antibody in human serum using protein L affinity purification and liquid chromatography/tandem mass spectrometry

(¹Natl. Inst. Health Sci., ²Ig-M, ³Ajinomoto, ⁴LSI Medience, ⁵CMIC Pharma Science, ⁶Takeda Pharm., ⁷TOWA Pharm.)
^oNoritaka Hashii¹, Yoko Hiruta¹, Yoshiko Tousaka¹, Shinko Hata², Naoyuki Yamada³, Hiroshi Itaya³, Yoshimi Kikuchi³, Kouji Arai⁴, Masaki Hoshino⁴, Shinichirou Nitta⁴, Hiroki Wakabayashi⁴, Keiko Nakai⁴, Rieko Goto⁵, Toshio Teramura⁵, Hisao Shimizu⁶, Hisashi Fujita⁶, Fumihiro Jinno⁶, Satomi Sasahara⁷, Hidehisa Tachiki⁷, Takuo Suzuki¹, Noriko Katori¹, Yoshiro Saito¹, Akiko Ishii¹

Liquid chromatography/tandem mass spectrometry (LC/MS/MS) is becoming an important approach for therapeutic antibody assays as an alternative to the ligand-binding assay method. However, a bioanalytical method using LC/MS/MS includes complicated sample preparation processes, such as affinity purification and enzymatic digestion. In this study, we developed an accessible bioanalytical method using LC/MS/MS to quantify a therapeutic antibody in human serum. The method uses a versatile protein L affinity purification process and SIL-Fab as the internal standard. This method was validated in the range of 0.05–50 μg/ml with a precision and accuracy of 14.6% and 101.6%, respectively, for the lower limit of quantification sample (0.05 μg/ml). We believe that this method will be useful as a template method for bioanalysis of therapeutic antibodies in human serum.