The reduced graphene oxide (rGO) supported cobalt oxide nanocatalysts were prepared by the conventional precipitationand hydrothermal method. The as-prepared rGO-Co3O4 was characterized by the XRD, Raman spectrum, S...The reduced graphene oxide (rGO) supported cobalt oxide nanocatalysts were prepared by the conventional precipitationand hydrothermal method. The as-prepared rGO-Co3O4 was characterized by the XRD, Raman spectrum, SEM, TEM, N2-sorption,UV-Vis, XPS and H2-TPR measurements. The results show that the spinel cobalt oxide nanoparticles are highly fragmented on therGO support and possess uniform particle size, and the as-prepared catalysts possess high specific surface area and narrow pore sizedistribution. The catalytic properties of the as-prepared rGO-Co3O4 catalysts for CO oxidation were evaluated through acontinuous-flow fixed-bed microreactor-gas chromatograph system. The catalyst with 30% (mass fraction) reduced graphene oxideexhibits the highest activity for CO complete oxidation at 100 ℃.展开更多
AIM: To recombine the human alpha B-crystallin(αBcrystallin) using gene cloning technology and prokaryotic expression vector and confirm the biological activity of recombinant human αB-crystallin. METHODS: Cloning t...AIM: To recombine the human alpha B-crystallin(αBcrystallin) using gene cloning technology and prokaryotic expression vector and confirm the biological activity of recombinant human αB-crystallin. METHODS: Cloning the human αB-crystallin cDNA according to the nucleotide sequence of the human αBcrystallin, constructing the pET-28/CRYAB prokaryotic expression plasmid by restriction enzyme digestion method, and stably expressing transformed into the Escherichia coli(E. coli) DH5 alpha. The recombinant human αB-crystallin was purified by Q sepharose. By enzyme digestion analysis, Western blotting and sequencing, the recombinant human αB-crystallin was identified and the activity of its molecular protein was detected.RESULTS: Compared with the gene bank(GeneBank), the cloned human sequence of human αB-crystallin cDNA has the same open reading frame. Identification and sequencing of the cloned human αB-crystallin cDNA in prokaryotic expression vector confirmed the full length sequence, and the vector was constructed successfully. The E. coli containing plasmid pET-28/CRYAB induced by isopropyl-β-D-thiogalactoside successfully expressed the human αB-crystallin. Insulin confirmed that the recombinant human αB-crystallin has a molecular chaperone activity. CONCLUSION: The prokaryotic expression vector pET-28/CRYAB of recombinant human αB-crystallin issuccessfully constructed, and the recombinant human αBcrystallin with molecular chaperone activity is obtained, which lay a foundation for the research and application of the recombinant human αB-crystallin and its chaperone activity.展开更多
AIM:To describe the clinical heterogeneity of patients with novel mutations in BEST1.METHODS:All the members in the two Chinese families underwent detailed clinical evaluations including best-corrected visual acuity,s...AIM:To describe the clinical heterogeneity of patients with novel mutations in BEST1.METHODS:All the members in the two Chinese families underwent detailed clinical evaluations including best-corrected visual acuity,slit-lamp examination,applanation tonometry,and dilated fundus examination.Fundus autofluorescence,fundus fluorescein angiography,spectral-domain optical coherence tomography,electrooculography,and electroretinogram were also performed.Genomic DNA was extracted from venous blood for all the participants.The targeted next-generation sequencing of inherited retinal disease-associated genes was conducted to identify the causative mutation.RESULTS:A novel BEST1 missense mutation c.41T>C(p.Leu14Ser) was identified in Family 1.It was co-segregated with the phenotype of best vitelliform macular dystrophy(BVMD) and bioinformatics analysis confirmed it was harmful.Another novel BEST1 frameshift mutation c.345_(3)46insGGCAAGGACG(p.Glu119Glyfs*116) and a novel USH2A missense mutation c.12560G>A,p.Arg4187 His were identified in family 2 with retinitis pigmentosa(RP),which might interact and lead to the phenotype of RP.CONCLUSION:Two novel mutations in the BEST1 gene in two unrelated families with distinct phenotypes and BEST1 mutation accompanied with USH2A mutation would result in RP,which could be enormously helpful in understanding the pathogenesis of the inherited retinal disease caused by a BEST1 mutation.展开更多
基金Projects(51404097,51504083,21404033)supported by the National Natural Science Foundation of ChinaProject(2016M592290)supported by China Postdoctoral Science Foundation+5 种基金Project(NSFRF1606)supported by the Fundamental Research Funds for the Universities of Henan Province,ChinaProjects(J2016-2,J2017-3)supported by Foundation for Distinguished Young Scientists of Henan Polytechnic University,ChinaProject(16A150009)supported by the Key Scientific Research Project for Higher Education of Henan Province,ChinaProject(166115)supported by the Postdoctoral Science Foundation of Henan Province,ChinaProject(17HASTIT029)supported by Program for Science&Technology Innovation Talents in Universities of Henan Province,ChinaProjects(162300410113,162300410119)supported by Natural Science Foundation of Henan Province of China
文摘The reduced graphene oxide (rGO) supported cobalt oxide nanocatalysts were prepared by the conventional precipitationand hydrothermal method. The as-prepared rGO-Co3O4 was characterized by the XRD, Raman spectrum, SEM, TEM, N2-sorption,UV-Vis, XPS and H2-TPR measurements. The results show that the spinel cobalt oxide nanoparticles are highly fragmented on therGO support and possess uniform particle size, and the as-prepared catalysts possess high specific surface area and narrow pore sizedistribution. The catalytic properties of the as-prepared rGO-Co3O4 catalysts for CO oxidation were evaluated through acontinuous-flow fixed-bed microreactor-gas chromatograph system. The catalyst with 30% (mass fraction) reduced graphene oxideexhibits the highest activity for CO complete oxidation at 100 ℃.
基金Supported by National Natural Science Foundation of China Grant (No.81270996)Science and Technology Project Foundation of Hainan Province (No.ZDYF201631)Health Science and Technology Innovation Project Foundation of Sanya (No.2016YW22)
文摘AIM: To recombine the human alpha B-crystallin(αBcrystallin) using gene cloning technology and prokaryotic expression vector and confirm the biological activity of recombinant human αB-crystallin. METHODS: Cloning the human αB-crystallin cDNA according to the nucleotide sequence of the human αBcrystallin, constructing the pET-28/CRYAB prokaryotic expression plasmid by restriction enzyme digestion method, and stably expressing transformed into the Escherichia coli(E. coli) DH5 alpha. The recombinant human αB-crystallin was purified by Q sepharose. By enzyme digestion analysis, Western blotting and sequencing, the recombinant human αB-crystallin was identified and the activity of its molecular protein was detected.RESULTS: Compared with the gene bank(GeneBank), the cloned human sequence of human αB-crystallin cDNA has the same open reading frame. Identification and sequencing of the cloned human αB-crystallin cDNA in prokaryotic expression vector confirmed the full length sequence, and the vector was constructed successfully. The E. coli containing plasmid pET-28/CRYAB induced by isopropyl-β-D-thiogalactoside successfully expressed the human αB-crystallin. Insulin confirmed that the recombinant human αB-crystallin has a molecular chaperone activity. CONCLUSION: The prokaryotic expression vector pET-28/CRYAB of recombinant human αB-crystallin issuccessfully constructed, and the recombinant human αBcrystallin with molecular chaperone activity is obtained, which lay a foundation for the research and application of the recombinant human αB-crystallin and its chaperone activity.
基金Supported by the Health Special Research Projects of Military Commission (No.19BJZ39)the Key Research Plan of Hainan Province (No.ZDYF2020031)。
文摘AIM:To describe the clinical heterogeneity of patients with novel mutations in BEST1.METHODS:All the members in the two Chinese families underwent detailed clinical evaluations including best-corrected visual acuity,slit-lamp examination,applanation tonometry,and dilated fundus examination.Fundus autofluorescence,fundus fluorescein angiography,spectral-domain optical coherence tomography,electrooculography,and electroretinogram were also performed.Genomic DNA was extracted from venous blood for all the participants.The targeted next-generation sequencing of inherited retinal disease-associated genes was conducted to identify the causative mutation.RESULTS:A novel BEST1 missense mutation c.41T>C(p.Leu14Ser) was identified in Family 1.It was co-segregated with the phenotype of best vitelliform macular dystrophy(BVMD) and bioinformatics analysis confirmed it was harmful.Another novel BEST1 frameshift mutation c.345_(3)46insGGCAAGGACG(p.Glu119Glyfs*116) and a novel USH2A missense mutation c.12560G>A,p.Arg4187 His were identified in family 2 with retinitis pigmentosa(RP),which might interact and lead to the phenotype of RP.CONCLUSION:Two novel mutations in the BEST1 gene in two unrelated families with distinct phenotypes and BEST1 mutation accompanied with USH2A mutation would result in RP,which could be enormously helpful in understanding the pathogenesis of the inherited retinal disease caused by a BEST1 mutation.