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. 1993 Oct;36(10):1224-32.

Synthesis and expression in Escherichia coli of a human neutrophil activating protein-1/interleukin-8 gene

D Y Jin  1 , R H Xu, Y Zhou, P Wang, Y D Hou
Affiliations
  • PMID: 8136035

Synthesis and expression in Escherichia coli of a human neutrophil activating protein-1/interleukin-8 gene

D Y Jin et al. Sci China B. 1993 Oct.

Abstract

The complete gene coding for human neutrophil activating protein-1/interleukin-8 was synthesized using a semi-chemical semi-enzymatic method. The synthetic gene was then overexpressed in Escherichia coli under the temperature-regulated control of the PRPL tandem promoters. As determined by SDS-PAGE and densitometry, the overexpressed protein comprised up to 18.5% and 10.9% of the total soluble protein in E. coli cells grown in shake flasks and in batch fermentation, respectively. The recombinant NAP-1/IL-8 was then purified to > 95% homogeneity by gel filtration and cation exchange chromatography. The purified protein appeared as a single band on the SDS-PAGE gel and possessed potent chemotactic activity in the concentration of < 10 ng/ml, as assayed by the agarose plate method. An early skin reactivity was also observed when the pure NAP-1/IL-8 was injected subcutaneously into the rabbits. The N-terminal 36 amino acid sequence of the recombinant NAP-1/IL-8 was determined using the Edman method and was shown to be identical to that of the native protein.

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