Purification and Some Physicochemical Properties of Staphylococcal Enterotoxin E
作者： Concordia R. Borja , Ellen Fanning , I-Yih Huang , Merlin S. Bergdoll
DOI: 10.1016/S0021-9258(19)45450-1
关键词: Polyacrylamide gel electrophoresis 、 Chromatography 、 Sephadex 、 Gel electrophoresis 、 Size-exclusion chromatography 、 Ion chromatography 、 Amino acid 、 Enterotoxin 、 Threonine 、 Chemistry
摘要: Abstract Enterotoxin E produced by Staphylococcus aureus strain FRI (Food Research Institute)-326 was purified cation exchange chromatography on carboxymethylcellulose, gel filtration through superfine Sephadex G-75, and in 6 m urea with G-75. The toxin appears to be nearly homogeneous paper, starch gel, polyacrylamide electrophoresis double diffusion tests. It is a simple, colorless, antigenic protein. Its molecular weight determined 29,600 ± 500 sucrose density gradient centrifugation, sieve G-100, sodium dodecyl sulfate-polyacrylamide electrophoresis. toxicity reaction its specific antibody are destroyed extreme acidic (pH 2) basic 12) conditions. Urea-treated enterotoxin retains toxic activity after removal of the denaturing agent. consists 259 amino acid residues contains no free sulfhydryl groups. End group analysis showed serine NH2-terminal threonine COOH-terminal acid.
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