The tetrazole analogues have been synthesized from fluorenylmethoxycarbonyl (Fmoc)- protected amino acids by three steps. The structures of the analogues were characterized by HPLC-MS, 1H NMR and 13C NMR.
Based on the different hydrophobicities of the intermediates of proteins the various conformational intermediates of the refolding of a-amylase originally denatured with 8.0 mol/L urea solution were separated with hig...Based on the different hydrophobicities of the intermediates of proteins the various conformational intermediates of the refolding of a-amylase originally denatured with 8.0 mol/L urea solution were separated with high performance hydrophobic interaction chromatography(HPHIC). Compared to the separation of the same intermediates with weak anion exchange chromatography and size-exclusion chromatography the result obtained with HPHIC is the best It would be expected that HPHIC may be a strongly potential tool to separate intermediates of some proteins which cannot be, or cannot completely be refolded by HPHIC.展开更多
Monodisperse poly (chloromethylstyrene divinylbenzene) particles were prepared by a two-step swelling method. It was demonstrated that the packings have comparative advantages for biopolymer separation with high colum...Monodisperse poly (chloromethylstyrene divinylbenzene) particles were prepared by a two-step swelling method. It was demonstrated that the packings have comparative advantages for biopolymer separation with high column efficiency, low interstitial volume and low back pressure to the packings prepared with suspension polymerization method. Using size exclusionchromatography and weak ion exchange chromatography as examples, it was shown that these packings could be modified chemically more easily than poly (styrene divinylbenzene) packings.展开更多
The thermal behaviors of five proteins in hydrophobic interaction chromatography (HIC) were investigated in the temperature range from 0 to 50℃. The thermodynamic parameters (?H°, ?S°, ?Cp°and ?G°...The thermal behaviors of five proteins in hydrophobic interaction chromatography (HIC) were investigated in the temperature range from 0 to 50℃. The thermodynamic parameters (?H°, ?S°, ?Cp°and ?G°) of these proteins in the process of retention and unfolding were determined. The existence of enthalpy and entropy convergence with temperature was confirmed. The differences of the isoentropic and isoenthalpic temperatures for protein unfolding in HIC system from the traditional solution were elucidated.展开更多
基金supported by the National Natural Science Foundation of China(No.20575052)Science Foundation of Northwest University(No.04NW42).
文摘The tetrazole analogues have been synthesized from fluorenylmethoxycarbonyl (Fmoc)- protected amino acids by three steps. The structures of the analogues were characterized by HPLC-MS, 1H NMR and 13C NMR.
文摘Based on the different hydrophobicities of the intermediates of proteins the various conformational intermediates of the refolding of a-amylase originally denatured with 8.0 mol/L urea solution were separated with high performance hydrophobic interaction chromatography(HPHIC). Compared to the separation of the same intermediates with weak anion exchange chromatography and size-exclusion chromatography the result obtained with HPHIC is the best It would be expected that HPHIC may be a strongly potential tool to separate intermediates of some proteins which cannot be, or cannot completely be refolded by HPHIC.
文摘Monodisperse poly (chloromethylstyrene divinylbenzene) particles were prepared by a two-step swelling method. It was demonstrated that the packings have comparative advantages for biopolymer separation with high column efficiency, low interstitial volume and low back pressure to the packings prepared with suspension polymerization method. Using size exclusionchromatography and weak ion exchange chromatography as examples, it was shown that these packings could be modified chemically more easily than poly (styrene divinylbenzene) packings.
文摘The thermal behaviors of five proteins in hydrophobic interaction chromatography (HIC) were investigated in the temperature range from 0 to 50℃. The thermodynamic parameters (?H°, ?S°, ?Cp°and ?G°) of these proteins in the process of retention and unfolding were determined. The existence of enthalpy and entropy convergence with temperature was confirmed. The differences of the isoentropic and isoenthalpic temperatures for protein unfolding in HIC system from the traditional solution were elucidated.
基金supported by National Natural Science Foundation of China(No.20975080)Program for New Century Excellent Talents in University(No.NCET-08-0892)+1 种基金Major State Basic Research Development Program of China(No.2009CB26608)Natural Science Foundation of Ningxia Province(No.NZ0914)
