Abstract
Binding of nucleotides, a tetrapolyphosphate, and NAD+ to purified toxin A of Clostridium difficile was determined by monitoring changes in intrinsic fluorescence following excitation at 280 nm, and recording emissions at 340 nm. Binding was specific for concentrations over the range 5 to 100 microM for ATP, GTP, and their respective non-hydrolysable analogues AMP-PNP and Gpp(NH)p, tetrapolyphosphate and NAD+.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Bacterial Toxins / metabolism*
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Binding Sites
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Clostridioides difficile / metabolism*
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Enterotoxins / chemistry
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Enterotoxins / metabolism*
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Guanosine Triphosphate / metabolism
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Molecular Sequence Data
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NAD / metabolism*
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Nucleotides / metabolism*
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Protein Conformation
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Spectrometry, Fluorescence
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Tryptophan / chemistry
Substances
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Bacterial Toxins
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Enterotoxins
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Nucleotides
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tcdA protein, Clostridium difficile
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NAD
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Guanosine Triphosphate
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Tryptophan
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Adenosine Triphosphate