ABSTRACT
This paper presents a one-step photochemical method for the preparation of CdS/Poly(MMA-co-MAA) composite photocatalyst, based on the concept of simultaneous photocatalytic polymerization of organic monomers during UV-light induced formation of CdS. The preparation is carried out in an aqueous solution of Na2S2O3, CdSO4, methyl methacrylate (MMA) and methacrylic acid (MAA), under a UV lamp. The continuously formed CdS particles with photocatalytic activity act the role of initiator to directly initiate the copolymerization of MMA and MAA, resulting in the inâ situ formation of the composite and full contact of the CdS particles with the oxygen-containing groups in the polymer. Taking the photocatalytic degradation of methylene blue as a case study, the composite exhibited significantly higher activity under simulated solar light compared to the pure CdS. By analysis on various data, the enhanced photocatalytic activity is attributed to the enhanced visible light absorption, and especially the high electron-hole separation efficiency caused by the electrostatic interaction between photogenerated holes and carbonyl oxygen atoms with negatively charged features. Furthermore, the composite displays excellent sunlight activity and recyclability, suggesting its potential for practical applications. Such a one-step construction strategy relying only on photo-energy is green, low-cost and promising in obtaining high-performance semiconductor/polymer composite photocatalysts.
ABSTRACT
Improving yield is one of the most important targets of sesame breeding. Identifying quantitative trait loci (QTLs) of yield-related traits is a prerequisite for marker-assisted selection (MAS) and QTL/gene cloning. In this study, a BC1 population was developed and genotyped with the specific-locus amplified fragment (SLAF) sequencing technology, and a high-density genetic map was constructed. The map consisted of 13 linkage groups, contained 3528 SLAF markers, and covered a total of 1312.52 cM genetic distance, with an average distance of 0.37 cM between adjacent markers. Based on the map, 46 significant QTLs were identified for seven yield-related traits across three environments. These QTLs distributed on 11 linkage groups, each explaining 2.34-71.41% of the phenotypic variation. Of the QTLs, 23 were stable QTLs that were detected in more than one environment, and 20 were major QTLs that explained more than 10% of the corresponding phenotypic variation in at least one environment. Favorable alleles of 38 QTLs originated from the locally adapted variety, Yuzhi 4; the exotic germplasm line, BS, contributed favorable alleles to only 8 QTLs. The results should provide useful information for future molecular breeding and functional gene cloning. Supplementary Information: The online version contains supplementary material available at 10.1007/s11032-021-01236-x.
ABSTRACT
OBJECTIVE: To investigate the mechanism by which heat shock protein 90 (HSP90) regulates 26S proteasome in hyperthermia. METHODS: Hyperthermic HepG2 cell models established by exposure of the cells to 42 degrees celsius; for 3, 6, 12, and 24 h were examined for production of reactive oxygen species (ROS) and cell proliferation, and the changes in Hsp90α and 26S proteasome were analyzed. RESULTS: ROS production in the cells increased significantly after hyperthermia (F=28.958, P<0.001), and the cell proliferation was suppressed progressively as the heat exposure time extended (F=621.704, P<0.001). Hyperthermia up-regulated Hsp90α but decreased the expression level (F=164.174, P<0.001) and activity (F=133.043, P<0.001) of 26S proteasome. The cells transfected with a small interfering RNA targeting Hsp90α also showed significantly decreased expression of 26S proteasome (F=180.231, P<0.001). CONCLUSION: The intracellular ROS production increases as the hyperthermia time extends. Heat stress and ROS together cause protein denature, leading to increased HSP90 consumption and further to HSP90 deficiency for maintaining 26S proteasome assembly and stability. The accumulation of denatured protein causes unfolded protein reaction in the cells to eventually result in cell death.
