Mirza U A, Cohen S L, Chait B T
Rockefeller University, New York, New York 10021.
Anal Chem. 1993 Jan 1;65(1):1-6. doi: 10.1021/ac00049a003.
A simple and effective device for investigating heat-induced denaturation of proteins by electrospray ionization mass spectrometry is described. Results are presented for the denaturation as a function of temperature and solution pH of bovine ubiquitin and bovine cytochrome c. These results are in concert with and extend the earlier results of LeBlanc et al. (Org. Mass Spectrom. 1991, 26, 831). The cooperative effects of pH and temperature on the denaturation of ubiquitin and cytochrome c were investigated. Electrospray ionization mass spectrometry is also shown to be a useful probe of the reversibility of heat-induced denaturation of proteins. Finally, it is demonstrated that heat-induced denaturation can be used to improve the mass spectrometric response of proteins that do not normally yield useful spectra when the solubilized protein is electrosprayed at ambient temperatures.
本文描述了一种通过电喷雾电离质谱法研究热诱导蛋白质变性的简单有效装置。给出了牛泛素和牛细胞色素c变性随温度和溶液pH值变化的结果。这些结果与LeBlanc等人（《有机质谱》，1991年，第26卷，第831页）早期的结果一致，并对其进行了扩展。研究了pH值和温度对泛素和细胞色素c变性的协同作用。电喷雾电离质谱法也被证明是研究热诱导蛋白质变性可逆性的有用探针。最后，证明了热诱导变性可用于改善那些在环境温度下将溶解的蛋白质进行电喷雾时通常无法产生有用光谱的蛋白质的质谱响应。
