Five guanido packings of affinity chromatography for the separation of urokinase have been synthesized. The separation characteristics and the effect of matrix and ligands on them have been studied. The guanidine deri...Five guanido packings of affinity chromatography for the separation of urokinase have been synthesized. The separation characteristics and the effect of matrix and ligands on them have been studied. The guanidine derivative is a fine ligand, the packings with ligand of arginine are much better than that with ligand of p-ABZ. The polyepoxypropyl methacrylate microsphere is a good matrix. The comprehensive function of packings with ligand of arginine and matrix of polyepoxypropyl methacrylate microsphere is more excellent than Sepharose-p-ABZ.展开更多
The synthesis of packing of oxygen-ethane as end-ligand bonded to silica andseparation for recombinant human interferons(rhIFN) in high-performance hydrophobicinteraction chromatography has been studied in this paper....The synthesis of packing of oxygen-ethane as end-ligand bonded to silica andseparation for recombinant human interferons(rhIFN) in high-performance hydrophobicinteraction chromatography has been studied in this paper. It was showed that the packingsynthesized was not only suitable for separating standard proteins, but also for different rhIFNs,i. e., rhIFN-αA expressed in yeast, rhIFN-αA and rh1FN-γ in E. colt. The purify of threerhIFNs purified by one-step HPHIC, which rhIFN-γ expressed in E. colt was recognized as80%, rhIFN-αA expressed in yeast as 70%, and rhIFN-αA expressed in E. colt as 30%, wasmore than that of other chromatography besides affinity chromatography.展开更多
A downstream purification procedure for recombinant human interferon-γ(rhIFN-γ) expressed in E. coli was described. An essentially two-step chromatographic purification procedure, i. e., size exclusion chromatograph...A downstream purification procedure for recombinant human interferon-γ(rhIFN-γ) expressed in E. coli was described. An essentially two-step chromatographic purification procedure, i. e., size exclusion chromatography(SEC) and high-performance hydrophobic in-teraction chromatography (HPHIC), was used for purification of homogeneity of rhIFN-γ from the inclusion body. The specific activity of purified rhIFN-Y was 1.0×108 IU/mg pro-tein. The product of purification rhIFN-γ was analyzed by an analytical high-per formance SEC and a significant sigle symmetrical peak had been found. The purity of purified rhIFN-Y was greater than 95% from analysis, determination by analytical HPSEC and SDS-PAGE with Coomssie Blue. The molecular weight was ca. 15 000. It was shown that this procedure was an effective method for purifying rhIFN-γ.展开更多
文摘Five guanido packings of affinity chromatography for the separation of urokinase have been synthesized. The separation characteristics and the effect of matrix and ligands on them have been studied. The guanidine derivative is a fine ligand, the packings with ligand of arginine are much better than that with ligand of p-ABZ. The polyepoxypropyl methacrylate microsphere is a good matrix. The comprehensive function of packings with ligand of arginine and matrix of polyepoxypropyl methacrylate microsphere is more excellent than Sepharose-p-ABZ.
文摘The synthesis of packing of oxygen-ethane as end-ligand bonded to silica andseparation for recombinant human interferons(rhIFN) in high-performance hydrophobicinteraction chromatography has been studied in this paper. It was showed that the packingsynthesized was not only suitable for separating standard proteins, but also for different rhIFNs,i. e., rhIFN-αA expressed in yeast, rhIFN-αA and rh1FN-γ in E. colt. The purify of threerhIFNs purified by one-step HPHIC, which rhIFN-γ expressed in E. colt was recognized as80%, rhIFN-αA expressed in yeast as 70%, and rhIFN-αA expressed in E. colt as 30%, wasmore than that of other chromatography besides affinity chromatography.
文摘A downstream purification procedure for recombinant human interferon-γ(rhIFN-γ) expressed in E. coli was described. An essentially two-step chromatographic purification procedure, i. e., size exclusion chromatography(SEC) and high-performance hydrophobic in-teraction chromatography (HPHIC), was used for purification of homogeneity of rhIFN-γ from the inclusion body. The specific activity of purified rhIFN-Y was 1.0×108 IU/mg pro-tein. The product of purification rhIFN-γ was analyzed by an analytical high-per formance SEC and a significant sigle symmetrical peak had been found. The purity of purified rhIFN-Y was greater than 95% from analysis, determination by analytical HPSEC and SDS-PAGE with Coomssie Blue. The molecular weight was ca. 15 000. It was shown that this procedure was an effective method for purifying rhIFN-γ.
