Expression of a biologically active fragment of human IgE epsilon chain in Escherichia coli.

AUTOR(ES)

Liu, F T

RESUMO

cDNA corresponding to human IgE heavy (epsilon) chain mRNA was cloned from human IgE-secreting myeloma U266 cells. Partial nucleotide sequence analysis demonstrated that the cloned cDNA contained the coding region for about two-thirds of the CH2 and all of the CH3 and CH4 domains as well as the 3'-untranslated region. This epsilon cDNA was inserted into expression vector pUC7 and expression of an epsilon-chain fragment in Escherichia coli was demonstrated by protein blot analysis using 125I-labeled goat anti-human IgE as probe. The expression product was purified on a column of goat anti-human IgE-conjugated Sepharose 4B and the polypeptide was found to retain binding activity to human basophils.

Documentos Relacionados

• Properties of a human immunoglobulin epsilon-chain fragment synthesized in Escherichia coli.
• Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc epsilon RI alpha chain.
• The expression of biologically active cholera toxin in Escherichia coli.
• Expression of human immunoglobulin E epsilon chain cDNA in E. coli.
• Blocking of passive sensitization of human mast cells and basophil granulocytes with IgE antibodies by a recombinant human epsilon-chain fragment of 76 amino acids.