Elevated degradation of di-n-butyl phthalate by activating peroxymonosulfate over GO-CoFe_(2)O_(4)composites:Synergistic effects and mechanisms

Rational design of heterogeneous catalysts with high activity and stability is crucial in peroxymonosulfate(PMS)-based oxidation treatment of wastewater.Herein,the graphite oxide-cobalt ferrite(GOCoFe_(2)O_(4))composite was constructed,and its morphological,component and structural characteristics were thoroughly examined,respectively.GO-CoFe_(2)O_(4)obviously boosted PMS catalytic performance on di-n-butyl phthalate removal(DBP,RpBp=90%,Roc=37%),which indicated by the first-order kinetic constant(kpBp=0.060 min^(-1))being roughly 4 times than pure CoFe_(2)O_(4)(kpBp=0.015 min-1).The fabrication of GO-CoFe_(2)O_(4)brought the favorable stability and repeatability up to six cycles.Moreover,the method of batch dosing catalyst was creatively proposed to improve the PMS utilization efficiency.The coupling of GO enhanced the dispersion of CoFe_(2)O_(4)particles to obtain sufficient active sites,additionally,the plentiful C=O groups and free-flowing electrons on GO promoted GO-CoFe_(2)O_(4)to coordinate a redox process during PMS activation.With the aid of theoretical calculations,GO-CoFe_(2)O_(4)was revealed to exhibit a strong affinity toward PMS adsorption,where PMS spontaneously dissociated into sulfate radical(SO_(4)^(·-)),hydroxyl radical(^(·)OH)and singlet oxygen(^(1)O_(2)),acting as the reactive oxygen species(ROSs).Electrons cycling between Co,Fe and O species ensured continuous ROSs generation and excellent catalytic performance.

The binding of the anticoagulation factor I from the venom of Agkistrodon acutus to activated factor X

Anticoagulation factor Ⅰ (ACF Ⅰ) from the venom of Agkistrodon acutus prolonged plasma prothrombin time (PPT) with dose-dependent manner and exhibited marked anticoagulant activity only at the concentration higher than its critical concentration (12 nmol/L). It was discovered that ACF Ⅰ formed a 1:1 complex with activated coagulation factor (FXa) in the presence of Ca2+ ions by the method of polyacrylamide gel electrophoresis. Both native ACF I and decalcified ACF Ⅰ failed to form complexes with FXa in the absence of Ca2+. Sr2+ ions were able to replace Ca2+ ions in the binding of ACF I to FXa, but both Ba2+ ions and Tb3+ ions were ineffective. ACF Ⅰ was a new member of the IX/X-bp family in the C-type lectin superfamily, and had a amino acid composition similar to the other members of this family. It was composed of 251 amino acid residues with a molecular weight of 29 603.6 u on non-reducing condition, determined by MALDI-TOF-MS, and a molecular weight of 14.7 ku on reducing condition,