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β-Conglycinin (β-CG), a major soy protein, has been associated with the reduction of body fat and triglycerides in the blood. Quantitation of the α, α, and β subunits in β-CG is desirable to establish the functional properties of β-CG in soybean. Therefore, in this study, we used the Jess System, a capillary electrophoresis-based immunoassay system, for quantifying β-CG in soybean foods. The validity of this method was confirmed using soybeans and processed soy milk. The within-laboratory reproducibility of the total β-CG amount was < 15 %, and its trueness was > 80 %. The β-CG content in the commercially available soybeans, Kori-tofu, soy milk, soy yogurt, Okara powder, and soy meat was determined to be 40.3-148.5, 65.2-97.2, 6.1-7.8, 3.5, 18.0, and 57.5 mg/g, respectively. For the first time in the literature, this method enables the quantitation of individual subunits of β-CG, despite the large variation in the amount of each subunit. [ABSTRACT FROM AUTHOR]

Foreign amylase addition to honey in an effort to disguise diastase activity has become a widespread form of food fraud. However, since there is no report on the investigation in Japan, we investigated foreign amylases in 67 commercial honeys in Japan. First, the α-glucosidase and diastase activities of honeys were measured, which revealed that only α-glucosidase activity was significantly low in several samples. As both enzymes are secreted from honeybee glands, it is unlikely that only one enzyme was inactivated during processing. Therefore, we suspected the presence of foreign amylase. α-Amylase in honey were assigned using protein analysis software based on LC-QTOF-MS. As a result, α-amylases from Aspergillus and Geobacillus were detected in 13 and 6 out of 67 honeys, respectively. To detect foreign amylases easily, we developed a cost-effective method using native PAGE. Conventional native PAGE failed to separate the α-amylase derived from honeybee and Geobacillus. However, when native PAGE was performed using a gel containing 1 % maltodextrin, the α-amylase from honeybee did not migrated in the gel and the α-amylase could be separated from the other two α-amylases. The results from this method were consistent with those of LC-QTOF-MS method, suggesting that the novel native PAGE method can be used to detect foreign amylases. [ABSTRACT FROM AUTHOR]

Activating mutations in KEAP1-NRF2 are frequently found in tumors of the lung, esophagus, and liver, where they are associated with aggressive growth, resistance to cancer therapies, and low overall survival. Despite the fact that NRF2 is a validated driver of tumorigenesis and chemotherapeutic resistance, there are currently no approved drugs which can inhibit its activity. Therefore, there is an urgent clinical need to identify NRF2-selective cancer therapies. To this end, we developed a novel synthetic lethal assay, based on fluorescently labeled isogenic wild-type and Keap1 knockout cell lines, in order to screen for compounds which selectively kill cells in an NRF2-dependent manner. Through this approach, we identified three compounds based on the geldanamycin scaffold which display synthetic lethality with NRF2. Mechanistically, we show that products of NRF2 target genes metabolize the quinone-containing geldanamycin compounds into more potent HSP90 inhibitors, which enhances their cytotoxicity while simultaneously restricting the synthetic lethal effect to cells with aberrant NRF2 activity. As all three of the geldanamycinderived compounds have been used in clinical trials, they represent ideal candidates for drug repositioning to target the currently untreatable NRF2 activity in cancer. [ABSTRACT FROM AUTHOR]