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Surface hydrophobicity and electrophoretic mobilities of staphylococcal exotoxins with special reference to toxic shock syndrome toxin‐1
Author(s) -
ERIKSSON KJELLOVE,
NAIDU A. SATYANARAYAN,
KILÁR FERENC,
WADSTRÖM TORKEL,
HJERTÉN STELLAN
Publication year - 1989
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1989.tb00521.x
Subject(s) - toxin , electrophoresis , chemistry , toxic shock syndrome , chromatography , enterotoxin , surface charge , microbiology and biotechnology , biochemistry , staphylococcus aureus , biology , escherichia coli , bacteria , gene , genetics
The surface hydrophobicities of eleven staphylococcal toxins were estimated and compared with those of standard proteins on an octyl agarose column by high‐performance hydrophobic‐interaction chromatography (HP‐HIC). Staphylococcal enterotoxins (SE) D, C3, C2, C1 and B showed a low surface hydrophobicity whereas alpha‐toxin and gamma‐toxin had a moderate surface hydrophobicity. SEA, toxic shock syndrome toxin‐1 (TSST‐1) and staphylococcal epidermolytic toxin (SET) showed high surface hydrophobicity and delta‐toxin was the most hydrophobic protein. The electrophoretic mobility of the toxins was determined by free zone electrophoresis (FZE). All toxins except SEC1 and one of the two SEA species showed negative charge at pH 8.6. Charge heterogeneity was observed in SEA, SEC1, SEC3 and TSST‐1: SEA and SEC1 had two overlapping components, whereas SEC3 and TSST‐1 were resolved into two distinct components. The mobilities of the two TSST‐1 components were estimated at ‐2.12 times 10 ‐5 and ‐3.60 times 10 ‐5 cm 2 v ‐1 s ‐1 , respectively, at 10 °C, and both fractions were immunologically indistinguishable as tested by specific TSST‐1 antibodies with ELISA. An asymmetric peak was obtained in hydrophobic‐interaction chromatography of TSST‐1, indicating heterogeneity.