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- W2392133600 abstract "Recombinant human-like collagen with a hexahistidine tail attacked to the carboxyl end could be easily purified by Metal Chelated Affinity Chromatography(MCAC). The affinity capability of MCAC with different immobilized metal ions(Zn2+、Cu2+ and Ca2+), the pH values of equilibrate buffer and different elution methods were compared. The results show that the effect of MCAC immobilized with Zn2+ is more effective than that with Cu2+ and Ca2+, the best equilibrate buffer pH is 7.5, and elution with 100mmol·L-1 ammonium chloride is better than that with pH gradient. The purity of recombinant human-like collagen could be 98%, recovery is 85.4%, purification fold is 3.4. The protein has the collagen features and has only one stripe on its SDS-PAGE electrophotogram. The molecular weight is 90ku and N terminus amino acids sequence is NH2-H-D-P-V-V-L-Q-R-R-D-W-E-N-P-G, which consistents with that deduced from DNA sequence." @default.
- W2392133600 created "2016-06-24" @default.
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- W2392133600 date "2005-01-01" @default.
- W2392133600 modified "2023-09-23" @default.
- W2392133600 title "Purification of Recombinant Human-like Collagen by Using Metal Chelated Affinity Chromatography" @default.
- W2392133600 hasPublicationYear "2005" @default.
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