OBSERVATION OF LARGE SUBUNIT PROTEIN COMPLEXES BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
OBSERVATION OF LARGE SUBUNIT PROTEIN COMPLEXES BY ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY
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DOI：
10.1002/jms.1190300127
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发表时间：
1995-01-01
影响因子：
2.3
通讯作者：
LOO, JA
中科院分区：
文献类型：
--
作者：
LOO, JA
采用电喷雾电离和磁扇形仪器的质谱法检测马肝醇脱氢酶（M（r）类似于80 000）和酵母醇脱氢酶（M（r）类似于147 000）和兔肌肉丙酮酸激酶（M（r）类似于232 000）的四聚体复合物的非共价结合二聚体亚基蛋白复合物的多电荷分子。丙酮酸激酶复合物的离子代表了质谱法分辨的最大的完整蛋白质复合物之一。大的气相复合物的溶剂化由质谱结果指示。
Mass spectrometry with electrospray ionization and a magnetic sector instrument was used to detect multiply charged molecules for the non-covalently bound dimeric subunit protein complexes of horse liver alcohol dehydrogenase (M(r) similar to 80 000) and the tetrameric complexes of yeast alcohol dehydrogenase (M(r) similar to 147 000) and rabbit muscle pyruvate kinase (M(r) similar to 232 000). Ions for the pyruvate kinase complex represent one of the largest intact protein complexes resolved by mass spectrometry. Solvation of the large gas phase complexes is indicated by the mass spectrometric results.