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. 2000 Feb-Mar;37(3-4):133-40.
doi: 10.1016/s0161-5890(00)00035-3.

Expression of the recombinant human immunoglobulin J chain in Escherichia coli

J Symersky  1 , J Novak, D T McPherson, L DeLucas, J Mestecky
Affiliations

Expression of the recombinant human immunoglobulin J chain in Escherichia coli

J Symersky et al. Mol Immunol. 2000 Feb-Mar.

Abstract

Selective transport of polymeric (p) immunoglobulins (Ig) of IgA and IgM isotypes into external secretions by pIg receptor-mediated mechanism depends on the incorporation of joining (J) chain into the polymers. Until now, availability of a free J chain for immunological and biophysical studies has been limited to preparations of denatured J chain forms with moderate yield. Here we report that a recombinant J chain (rJ) can be over-expressed as a soluble fusion protein with thioredoxin using a modified vector pET32 in Escherichia coli. An intact J chain was released by digestion with IgA1 protease from Neisseria gonorrhoeae and isolated in a good yield with immunological and biochemical properties similar to those of J chain obtained by chemical cleavage from pIgA.

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