LiVPO4F suffers problems of difficulty in synthesis and poor conductivity. To solve these,herein sub-micro spherical LiVPO4F/C is synthesized from a highly-reactive hollow VPO4/C sphere that is derived from a facile a...LiVPO4F suffers problems of difficulty in synthesis and poor conductivity. To solve these,herein sub-micro spherical LiVPO4F/C is synthesized from a highly-reactive hollow VPO4/C sphere that is derived from a facile and fast spray pyrolysis for the first time. Uniform carbon coating layer with a thickness of 5–8 nm is observed on the surface of the particles,helping to improve the electronic conductivity,suppress the particle growth and protect the particles from corrosion by the electrolyte. The particles are shaped as fine sub-micro spheres,which are beneficial for shortening the distance for Li+ transport. Rietveld refinement for the X-ray diffraction pattern of as-prepared sample shows high-purity triclinic LiVPO4F with an enlarged lattice volume,enabling faster Li+ transport in the prepared material. Accordingly,the resulted LiVPO4F/C demonstrates superior electrochemical properties,delivering 135.4,91.1 mA hg-1 at 1,40 C respectively,and remaining the capacity of 93.3 mA hg-1 after 500 cycles at 20 C with the retention of 95.0%. The method introduced here provides an efficient way to address the serious problems of preparing high-purity Li VPO4F with good conductivity.展开更多
The serological and biochemical characteriza-tion of porcine red blood cells (pRBCs) are similar to human red blood cells. Porcine erythrocytes are considered as an alternative source for human blood transfusion. But ...The serological and biochemical characteriza-tion of porcine red blood cells (pRBCs) are similar to human red blood cells. Porcine erythrocytes are considered as an alternative source for human blood transfusion. But there exist galactose-?,3-galactose antigens (Gal?,3Gal?, 4GalNAcR, abbreviated 酖al antigen) on pRBCs, which can induce anti-aGal antibodies in human serum. The aGal epitopes are the major antigen responsible for hyperacute rejection in xenotransfusion. In this study, recombined soy-bean -galactosidase (rS?GalE) was used to remove the aGal antigens from pPRCs for humanization. The results showed that aGal antigen was cleared by rS?GalE and the structure and function of rS?GalE treated pRBC were normal.展开更多
基金This work was supported by the National Natural Science Foundation of China(Grant Nos.51704332,51874360 and 51804344)the Program of Huxiang Young Talents(Grant No.2019RS2002)the Innovation and Entrepreneurship Project of Hunan Province,China(Grant No.2018GK5026)。
文摘LiVPO4F suffers problems of difficulty in synthesis and poor conductivity. To solve these,herein sub-micro spherical LiVPO4F/C is synthesized from a highly-reactive hollow VPO4/C sphere that is derived from a facile and fast spray pyrolysis for the first time. Uniform carbon coating layer with a thickness of 5–8 nm is observed on the surface of the particles,helping to improve the electronic conductivity,suppress the particle growth and protect the particles from corrosion by the electrolyte. The particles are shaped as fine sub-micro spheres,which are beneficial for shortening the distance for Li+ transport. Rietveld refinement for the X-ray diffraction pattern of as-prepared sample shows high-purity triclinic LiVPO4F with an enlarged lattice volume,enabling faster Li+ transport in the prepared material. Accordingly,the resulted LiVPO4F/C demonstrates superior electrochemical properties,delivering 135.4,91.1 mA hg-1 at 1,40 C respectively,and remaining the capacity of 93.3 mA hg-1 after 500 cycles at 20 C with the retention of 95.0%. The method introduced here provides an efficient way to address the serious problems of preparing high-purity Li VPO4F with good conductivity.
文摘The serological and biochemical characteriza-tion of porcine red blood cells (pRBCs) are similar to human red blood cells. Porcine erythrocytes are considered as an alternative source for human blood transfusion. But there exist galactose-?,3-galactose antigens (Gal?,3Gal?, 4GalNAcR, abbreviated 酖al antigen) on pRBCs, which can induce anti-aGal antibodies in human serum. The aGal epitopes are the major antigen responsible for hyperacute rejection in xenotransfusion. In this study, recombined soy-bean -galactosidase (rS?GalE) was used to remove the aGal antigens from pPRCs for humanization. The results showed that aGal antigen was cleared by rS?GalE and the structure and function of rS?GalE treated pRBC were normal.
