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Botulinum neurotoxins (BoNTs) are the most toxic substances known to humans. Endopeptidase-mass spectrometry (Endopep-MS) is used as a specific and rapid in vitro assay to detect BoNTs. In this assay, immunocaptured toxin cleaves a serotype-specific peptide substrate, and the cleavage products are then detected by MS. To further improve the sensitivity of(More)
VX is one of the most toxic chemical warfare agents. Its low volatility and its persistence in the environment raise the issue of long-term exposure risks, either by inhalation or by transdermal penetration. Therefore, a topic of acute interest is the fate of VX in preservative environmental surfaces. In this work, the fate of VX in asphalt pavement, a(More)
Botulinum neurotoxins (BoNTs) are the most toxic proteins in nature. Rapid and sensitive detection of BoNTs is achieved by the endopeptidase-mass spectrometry (Endopep-MS) assay. In this assay, BoNT cleaves a specific peptide substrate and the cleaved products are analyzed by MS. Here we describe the design of a new peptide substrate for improved detection(More)
Botulinum toxin was detected in patient serum using Endopeptidase-mass-spectrometry assay, although all conventional tests provided negative results. Antitoxin was administered, resulting in patient improvement. Implementing this highly sensitive and rapid assay will improve preparedness for foodborne botulism and deliberate exposure.
Botulinum neurotoxins (BoNTs) are the most toxic proteins in nature. Endopeptidase-mass-spectrometry (Endopep-MS) is used as a specific and rapid in-vitro assay to detect BoNTs. In this assay, immunocaptured toxin cleaves a serotype-specific-peptide-substrate, and the cleavage products are then detected by MS. Here we describe the design of a new peptide(More)
Blood serum of oncologic patients due to immunoglobulin involved in its composition, activates glycolysis in the soluble fraction of muscles when using starch, glycogen and glucose as substrates. The activation is registered under both aerobic and anaerobic conditions. When elucidating the immunoglobulin effect in a glycolytic chain under aerobic conditions(More)
Immunoglobulin G characteristic of malignant growth is studied for its effect on glycolysis in a dialyzed enzymic preparation from the rabbit muscles. A peptide-nature compound participating in immunoglobulin G activation of glycolysis is shown to transfer to dialysate in the process of the enzyme dialysis. The activation may involve cAMP, ADP, NADH.