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A CIRCULAR‐DICHROISM STUDY OF THE ENTEROTOXIN FROM CLOSTRIDIUM PERFRINGENS TYPE A
Author(s) -
GRANUM PER EINAR,
HARBITZ OLE
Publication year - 1985
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1985.tb00344.x
Subject(s) - enterotoxin , random coil , clostridium perfringens , circular dichroism , chemistry , sodium dodecyl sulfate , guanidine , urea , protein secondary structure , sodium , hydrochloride , chromatography , biochemistry , biology , organic chemistry , escherichia coli , bacteria , genetics , gene
Far‐UV circular‐dichroism spectra of the enterotoxin from Clostridium perfringens type A were recorded under different conditions, and conformational analysis was performed. The native enterotoxin (pH 6.8) was shown to contain about 80% pleated sheet, 20% random coil and no helix structure. By adding small amounts of the detergent sodium dodecyl sulfate (0–261 mol SDS/mol enterotoxin), the β‐sheet structure could gradually be changed to a more α‐helical structure. Treatment with 8 M urea resulted in limited alterations of the secondary structure of the enterotoxin, while heat treatment (60°C, 30 min), treatment with 6.5 M guanidine hydrochloride or 0.01 M NaOH led to a dramatic increase in the amount of random coil.