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Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometric analysis of phospholipase A 2 and fibrinolytic enzyme, two enzymes obtained from chinese Agkistrodon blomhoffii Ussurensis venom
Author(s) -
Sun MingZhong,
Ding Lan,
Ji YiPing,
Zhao DaQing,
Liu ShuYing,
Ni JiaZuan
Publication year - 1999
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19990215)13:3<150::aid-rcm471>3.0.co;2-6
Subject(s) - chemistry , chromatography , mass spectrometry , matrix assisted laser desorption/ionization , molecular mass , enzyme , mass spectrum , venom , time of flight mass spectrometry , desorption , ionization , ion , biochemistry , organic chemistry , adsorption
Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) was used to analyze two enzymes, phospholipase A 2 and fibrinolytic enzyme isolated from Chinese Agkistrodon blomhoffii Ussurensis venom. Using sinapinic acid as the matrix, positive ion mass spectra of the enzymes were obtained. In addition to the dominant protein [M+H] + ions, multimeric and multiply charged ions were also observed in the mass spectra. The higher the concentration of the enzymes, the more multiply charged polymer and multimeric ions were detected. Our results indicate that MALDI‐TOFMS can provide a rapid and accurate method for molecular weight determination of snake venom enzymes. Mass accuracies of 0.1 and 0.3% were achieved by analysis of highly dialyzed phospholipase A2 and fibrinolytic enzyme, and these results are much better than those obtained using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. MALDI‐TOFMS thus provides a reliable method to determine the purity and molecular weight of these enzymes, which are of potential use as therapeutants. Copyright © 1999 John Wiley & Sons, Ltd.