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1.
Environ Sci Technol ; 57(33): 12341-12350, 2023 08 22.
Artigo em Inglês | MEDLINE | ID: mdl-37552529

RESUMO

As the main anthropogenic source in open seas and coastal areas, ship emissions impact the climate, air quality, and human health. The latest marine fuel regulation with a sulfur content limit of 0.5% went into effect globally on January 1, 2020. Investigations of ship emissions after fuel switching are necessary. In this study, online field measurements at an urban coastal site and modeling simulations were conducted to detect the impact of ship emissions on air quality in the Greater Bay Area (GBA) in China under new fuel regulation. By utilizing a high mass-resolution single particle mass spectrometer, the vanadium(V) signal was critically identified and was taken as a robust indicator for ship-emitted particles (with relative peak area > 0.1). The considerable number fractions of high-V particles (up to 30-40% during ship plumes) indicated that heavy fuel oils via simple desulfurization or blending processes with low-sulfur fuels were extensively used in the GBA to meet the global 0.5% sulfur cap. Our results showed that ship-emitted particulate matter and NOx contributed up to 21.4% and 39.5% to the ambient, respectively, in the summertime, significantly affecting the air quality in the GBA. The sea-land breeze circulation also played an important role in the transport pattern of ship-emitted pollutants in the GBA.


Assuntos
Poluentes Atmosféricos , Poluição do Ar , Humanos , Poluentes Atmosféricos/análise , Emissões de Veículos/análise , Navios , Poluição do Ar/análise , Material Particulado/análise , China , Enxofre
2.
Int J Biol Macromol ; 139: 740-751, 2019 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-31377290

RESUMO

Frontal affinity chromatography (FAC) combined with enzyme has been widely used for drug screening. In this paper, the effect of target enzyme activity on screening of bioactive compounds was studied through applying FAC. Trypsin with different degree of inactivation were prepared as target enzyme by thermal denaturation. Their primary structure was identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and use Fourier transform infrared (FTIR) and ultraviolet-visible (UV-vis) spectroscopy to detect group structure. Ultimately, it was found that the main structure of enzyme with decreased activity remained unchanged. The oxymatrine and matrine which can interact with trypsin were selected to study their binding to trypsin with different activities in FAC. The results showed that oxymatrine and matrine had a significant difference in the breakthrough volume among seven kinds of columns prepared by trypsins with different activities, at the different concentration. It indicated that trypsins with different activities in FAC could combine with oxymatrine and matrine. The binding constant (Kd) variation between oxymatrine, matrine and trypsin with different activities are 5.520 ±â€¯0.038 and 3.577 ±â€¯0.071, within error range, which indicated that the activity of target enzyme with primary unchanged structure has no effect on screening of bioactive components by FAC.


Assuntos
Cromatografia de Afinidade , Tripsina/química , Alcaloides/química , Engenharia Genética , Glicerol/química , Temperatura Alta , Cinética , Espectroscopia de Ressonância Magnética , Microscopia Eletrônica de Varredura , Peptídeos/química , Quinolizinas/química , Silanos/química , Solventes/química , Espectrofotometria Ultravioleta , Espectroscopia de Infravermelho com Transformada de Fourier , Matrinas
3.
J Chromatogr Sci ; 53(6): 898-902, 2015 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-25362198

RESUMO

Trypsin is a serine protease that has been proposed as a potential therapeutic target for metabolic disorders and malignancy diseases, thus the identification of biomolecular interactions of compounds to trypsin could be of great therapeutic importance. In this study, trypsin was immobilized on a monolithic silica capillary column via sol-gel. The binding properties of four small molecules (daidzin, genistin, matrine and oxymatrine) to trypsin were examined using the trypsin affinity columns by frontal analysis. The results indicate that the matrine (dissociation constant, Kd = 7.904 µM) has stronger interaction with trypsin than the oxymatrine (Kd = 8.204 µM), whereas daidzin and genistin were nearly have no affinity with trypsin. The results demonstrated that the frontal affinity chromatography can be used for the direct determination of protein-protease inhibitor binding interactions and have several significant advantages, including easy fabricating, reproducible, minimal technological requirements and potential to become a reliable alternative for quantitative studies of biomolecular interactions.


Assuntos
Cromatografia de Afinidade/métodos , Enzimas Imobilizadas/metabolismo , Inibidores da Tripsina/análise , Inibidores da Tripsina/metabolismo , Tripsina/metabolismo , Alcaloides , Enzimas Imobilizadas/química , Isoflavonas , Cinética , Modelos Químicos , Quinolizinas , Dióxido de Silício , Tripsina/química , Inibidores da Tripsina/química , Matrinas
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