Loo J A
Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.
Mass Spectrom Rev. 1997 Jan-Feb;16(1):1-23. doi: 10.1002/(SICI)1098-2787(1997)16:1<1::AID-MAS1>3.0.CO;2-L.
Electrospray ionization mass spectrometry has been used to study protein interactions driven by noncovalent forces. The gentleness of the electrospray ionization process allows intact protein complexes to be directly detected by mass spectrometry. Evidence from the growing body of literature suggests that the ESI-MS observations for these weakly bound systems reflect, to some extent, the nature of the interaction found in the condensed phase. Stoichiometry of the complex can be easily obtained from the resulting mass spectrum because the molecular weight of the complex is directly measured. For the study of protein interactions, ESI-MS is complementary to other biophysical methods, such as NMR and analytical ultracentrifugation. However, mass spectrometry offers advantages in speed and sensitivity. The experimental variables that play a role in the outcome of ESI-MS studies of noncovalently bound complexes are reviewed. Several applications of ESI-MS are discussed, including protein interactions with metal ions and nucleic acids and subunit protein structures (quaternary structure).
电喷雾电离质谱已被用于研究由非共价力驱动的蛋白质相互作用。电喷雾电离过程的温和性使得完整的蛋白质复合物能够通过质谱直接检测。越来越多的文献证据表明，对于这些弱结合系统的电喷雾电离质谱观测在一定程度上反映了凝聚相中相互作用的性质。由于复合物的分子量是直接测量的，所以可以很容易地从所得质谱中获得复合物的化学计量。对于蛋白质相互作用的研究，电喷雾电离质谱与其他生物物理方法（如核磁共振和分析超速离心）互为补充。然而，质谱在速度和灵敏度方面具有优势。本文综述了在非共价结合复合物的电喷雾电离质谱研究结果中起作用的实验变量。讨论了电喷雾电离质谱的几种应用，包括蛋白质与金属离子和核酸的相互作用以及亚基蛋白质结构（四级结构）。
