期刊
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
卷 786, 期 1-2, 页码 153-159出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S1570-0232(02)00764-X
关键词
cloning; expression; purification; Escherichia coli; enhanced green fluorescent protein
In this report, we describe a two-step chromatographic procedure for the purification of His-tag EGFP by immobilized metal affinity expanded bed adsorption (IMAEBA) as the capture step and size exclusion chromatography as the polishing step. The use of proteins including a histidine-tag facilitates their subsequent purification after expression in many microorganisms. This meets the needs of scientific researchers as well as industrialists in purifying recombinant proteins. The procedure described allowed the obtention of 230 mg pure EGFP from 11 simple batch culture with a recovery of 90%. (C) 2002 Elsevier Science B.V. All rights reserved.
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