In vitro transformation of paralytic shellfish toxins in the clams Mya arenaria and Protothaca staminea
| Autor: | Allan Cembella, Neil W. Ross, M.D. Fast |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Carbamate
biology Ecology Toxin medicine.medical_treatment Protothaca staminea Plant Science Glutathione Carbamoylase Aquatic Science biology.organism_classification Bivalvia medicine.disease medicine.disease_cause paralytic shellfish toxins Shellfish poisoning chemistry.chemical_compound chemistry Biochemistry Biotransformation clamsc Mya arenaria medicine Paralytic shellfish poisoning Mollusca |
| DOI: | 10.1016/j.hal.2005.05.005 |
| Popis: | Dissected tissues of two clam species, the Pacific littleneck, Protothaca staminea, and soft-shell, Mya arenaria, were evaluated for in vitro conversion of paralytic shellfish poisoning (PSP) toxins. Tissue homogenates were incubated with purified PSP toxins to determine the time-course of toxin conversion. The effects of boiling and addition of a natural reductant (glutathione) on toxin conversion were also assessed. For P. staminea, the digestive gland showed the greatest capacity for biotransformation, followed by gill, but mantle, adductor muscle, and siphon tissues exhibited very low conversion. In this species, the production of decarbamoyl derivatives was much greater from low potency N-sulfocarbamoyl toxins than from carbamate analogues. Decarbamolyation exhibited apparent specificity for α-epimers of all toxin substrates and this reaction was inhibited by boiling. Glutathione-mediated desulfation was tissue specific and had apparent specificity for β-epimers. These observations on P. staminea suggest that the above reactions are enzyme-mediated. In contrast, there was little toxin conversion in M. arenaria homogenates, but even this low activity was heat-labile and thus likely enzyme-mediated. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|