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- W3147578951 abstract "BACKGROUNDAIM: To gain the NGAL protein with definite abundance and purity at last by the novel oncogene NGAL fusion expression in prokarote,purification by Ni 2+ _ metal chelate affinity chromatography and identification by MALDI-TOF-MS of its expression production. MATERIAL AND METHODS: pDsbA2.0-NGAL fusion expression vector was transformed to E.coli,induced to express with IPTG and productivity as well as soluˉbility of the expressed production were analyzed via SDS-PAGE.Then expressed production was purified by Ni 2+ _metal chelate affinity chromatography and identification byMALDI-TOF-MS. RESULTS: After induced expression of pDsbA2.0-NGAL fusion expression vector with IPTG,SDS-PAGE analysis presented the expressed NGAL fusion protein was high productivity with good solubility.Thepurity of expressed NGAL protein was more than95%after purified by Ni 2+ _metal chelate affinity chromatographyand identification by MALDI-TOF-MS indicated that the molecularweight error was only0.91‰between the purified NGAL protein and its theoretical one. CONCLUSION: By the novel oncogene NGAL fusion expression inprokarote,purification by Ni 2+ _metal chelate affinity chromatography and identification by MALDI-TOF-MS of its expression production,NGAL protein with definite abundance and electrophoresis purity was truely gained at last,which built up a good experimental material for the preparation of its antibody." @default.
- W3147578951 created "2021-04-13" @default.
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- W3147578951 date "2004-01-01" @default.
- W3147578951 modified "2023-09-29" @default.
- W3147578951 title "Purification by Ni~(2+)-Metal Chelate Affinity Chromatography and Identification of NGAL Protein" @default.
- W3147578951 hasPublicationYear "2004" @default.
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