Esterified estrogens/Methyltestosterone

ABSTRACTDiclofenac sodium (DS) is now recognized as an emerging pollutant, and is one of the most commonly discovered pharmaceuticals in water due to its extensive application in the clinic. This study examined the adsorption performance of a polystyrene-supported ionic liquid material (PS-[Nim][Cl]) for the removal of diclofenac sodium (DS) from water. The data from this study showed that maximum removal of DS can be achieved even in conditions with significant pH and temperature fluctuations. The adsorption process was rapid, more than 90% of DS could be removed within the first 10 min and adsorption equilibrium could be reached in just 30 min with a high removal efficiency (>99.9%). Adsorption reached saturation with a maximum adsorption capacity of approximately 785.2 mg/g. Moreover, the presence of K⁺, Na⁺, Ca²⁺, Mg²⁺, Cl^-, and H₂PO₄^- ions had little influence on DS adsorption, even when concentrations of these ions were 10,000 times higher than that of DS in water samples. The adsorbent also showed promising performance for the treatment of environmental water samples and groundwater containing DS.

The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for efficient strategies to improve OVT thermal stability is essential for improving egg product quality and processing suitability. Here, we investigated the effect of sulfate polysaccharide (dextran sulfate, DS) on heat-induced aggregation of OVT. We found that DS can effectively suppress amorphous aggregation of OVT at pH 7.0 after heating. Strikingly, the addition of 5 µM DS fully suppressed insoluble aggregates formation of 0.5 mg/mL OVT. Structure analysis confirmed that DS preserves nearly the entire secondary and tertiary structure of OVT during heating. The steric hindrance effect arising from strong electrostatic interactions between OVT and DS, coupled with reduced OVT hydrophobicity, is the underlying mechanism in suppressing protein-protein interactions, thus enhancing thermal stability. These findings suggest DS could act as protein stabilizers and chaperones, enhancing the thermostability of heat-sensitive proteins.