4 research outputs found

    Effects of gastric acid on euro coins: chemical reaction and radiographic appearance after ingestion by infants and children

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    Objectives: This study investigated whether coins of the new European currency (€) corrode when they are exposed to gastric acid, and whether this change can be detected radiographically. Methods: The eight different denominations of € coins were immersed for seven days in 0.15 N hydrochloride acid (HCl), which corresponds to the level of post-prandial gastric acid. A Swedish crown coin and three different Austrian schilling coins were used as controls. The coins were weighed and radiographed daily to evaluate visible corrosions and HCl was analysed daily for possible dissolved substances. Results: All coins lost weight within 24 hours after exposure to HCl. The 1, 2, and 5 € cent coins developed changes that were visible on radiographs. The weights of all coins decreased by 0.43% to 11.30% during one week. The dissolved substances measured in the HCl corresponded to the different metals and alloys of the coins, except for copper, which does not dissolve in HCl. The highest absolute weight loss was observed in the Swedish crown coin (0.67 g), and the highest relative weight loss in the 1 Austrian schilling coin (11.30%). The two € coins that showed the highest absolute and relative weight losses were the 2 € (0.54 g or 6.35%) and the 1 € (0.48 g or 6.39%) coin. Conclusions: A higher rate of toxicity for the new European coins compared with coins of other currencies is not expected, unless a massive coin ingestion occurs

    Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

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    Abstract Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to assist in the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). Our results indicate that during eEF1A synthesis, Chp1 is recruited to the ribosome with the help of the nascent polypeptide-associated complex (NAC), where it safeguards eEF1A biogenesis. Aberrant eEF1A production in the absence of Chp1 triggers instant proteolysis, widespread protein aggregation, activation of Hsf1 stress transcription and compromises cellular fitness. The expression of pathogenic eEF1A2 variants linked to epileptic-dyskinetic encephalopathy is protected by Chp1. Thus, eEF1A is a difficult-to-fold protein that necessitates a biogenesis pathway starting with dedicated folding factor Chp1 at the ribosome to protect the eukaryotic cell from proteostasis collapse
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