Detection of Specific Noncovalent Protein-fullerenols Complexes by Matrix-assisted Laser Desorption Ionization Mass Spectrometry

Abstract

Abstract: Matrix assisted laser desorption ionization(MALDI) mass spectrometry is difficult for the characterization of noncovalent complexes hitherto because of the limitations in acidic matrix, sample preparation, laser induced polymerization and adduct formation with matrix. Under our experimental conditions, sinapinic acid is used as a matrix, the specific noncovalent interactions of protein with fullerenols were observed by MALDImass spectrometry. Some mass spectrometric features, such as mass shifts, broad adduct peaks and stoichiometries, showed that the specific non covalent complexes between protein and fullerenols have been formed at a ratio of 1:4 for hemoglobin fullerenols or 1:1 for myoglobin fullerenols. The results implied that fullereneols could be used to protect partly hemoglobin from decomposition in acidic media, and therefore, it is possible to realize the molecular weight determination of a quaternary protein by MALDImass spectrometry via the addition of specific organic compound in the matrix.

Key words: Noncovalent interaction, Fullerenols, Myoglobin, Hemoglobin, Matrix assisted laser desorption ionization time of flight mass spectrometry

CLC Number:

O657.6

TrendMD:

SHE Yi-Min, JI Yi-Ping, HE Yu-Fan, LIU Shu-Ying . Detection of Specific Noncovalent Protein-fullerenols Complexes by Matrix-assisted Laser Desorption Ionization Mass Spectrometry[J]. Chem. J. Chinese Universities, 1998, 19(11): 1735.

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Detection of Specific Noncovalent Protein-fullerenols Complexes by Matrix-assisted Laser Desorption Ionization Mass Spectrometry

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