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KMID : 0380219940270040330
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 4 p.330 ~ p.334
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Simple Purification of Recombinant Human TNF-a by Conventional Chromatography
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Abstract
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Abstract:
@EN Recombinant human TNF(rhTNF) was purified from cell extracts of cloned E. coli BL21(DE3)/pT 7-TNF3,4 to apparent homogeneity by 80% ammonium sulfate precipitaion, DEAE-Sepharose ion exchange chromatography, and Sephacryl S-200 filtration
followed by
Bio-Gel P=100 gel filtration . The specific activity of this protein was increased approximately 30 fold during purification with an overall yield of 31%. In sodium dodecyl sulfate ge electrophoresis the recombinant human TNF migrates as a single
band
corresponding to a molecular weight of approximately 17 kDa. The molecular weight of the native protein as determined by Bio-Gel P-100 gel filtration was 48 kDa.
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KEYWORD
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