Analysis of quaternary protein ensembles by matrix assisted laser desorption/ionization mass spectrometry

被引:71
作者
Cohen, LRH [1 ]
Strupat, K [1 ]
Hillenkamp, F [1 ]
机构
[1] UNIV MUNSTER,INST MED PHYS & BIOPHYS,D-48149 MUNSTER,GERMANY
关键词
D O I
10.1016/S1044-0305(97)00148-7
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The intact noncovalent structure of the homo-oligomeric complexes of streptavidin (52 kDa), alcohol dehydrogenase (150 kDa), and beef Liver catalase (240 kDa) have been observed using the matrix 2,6-dihydroxyacetophenone in an organic solvent. Intact streptavidin tetramers could also be observed with ferulic acid and other hydroxyacetophenone derivatives. Intact complexes are observed only for the first shot al a given position, which may be due to physical segregation or precipitation of the noncovalent complexes at the crystal surface. This effect is independent of the macroscopic crystal structure or the type of substrate (hydrophobic versus hydrophilic). Observation of intact complexes is not affected by addition of less than 10 mM salts or buffers, and appears to be independent of the pH stability-range of the protein samples investigated. (C) 1997 American Society for Mass Spectrometry.
引用
收藏
页码:1046 / 1052
页数:7
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