Krone J R, Nelson R W, Dogruel D, Williams P, Granzow R
Department of Chemistry and Biochemistry, Arizona State University, Tempe 85287-1604, USA.
Anal Biochem. 1997 Jan 1;244(1):124-32. doi: 10.1006/abio.1996.9871.
Biomolecular interaction analysis (BIA) which utilizes surface plasmon resonance (SPR) detection of affinity-captured analytes has been interfaced with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI). Femtomole quantities of a peptide, myotoxin a, were detected by direct MALDI analysis of sensor chips used during BIA of a polyclonal anti-myotoxin a IgG/myotoxin a system. Further, different interactive surfaces (flow cells) present on a single biosensor were targeted individually for mass spectrometric analysis. System compatibility of the combined approach was demonstrated with sensitivities, detection limits, and analytical performances comparable to those intrinsic to the individual analyses. The combined approach unites the real-time capabilities of SPR-based BIA with the qualitative specificity of mass spectrometry.
利用表面等离子体共振（SPR）检测亲和捕获分析物的生物分子相互作用分析（BIA）已与基质辅助激光解吸/电离飞行时间质谱（MALDI）联用。通过对多克隆抗肌毒素a IgG/肌毒素a系统进行BIA期间使用的传感器芯片进行直接MALDI分析，检测到了飞摩尔量的一种肽——肌毒素a。此外，单个生物传感器上存在的不同相互作用表面（流通池）被分别作为质谱分析的目标。该联合方法的系统兼容性通过灵敏度、检测限和分析性能得到了证明，这些性能与单独分析的固有性能相当。该联合方法将基于SPR的BIA的实时功能与质谱的定性特异性结合在一起。
