Expression and purification of biologically active domain I of the human polymeric immunoglobulin receptor

Mary Ann Bakos, Steven Widen, Randall M. Goldblum

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Previous studies using proteolytic fragments and synthetic peptides have indicated that domain I of human polymeric immunoglobulin receptor (PlgR) is necessary for ligand binding. The expression in E. coli, and subsequent IgM-affinity purification of domain I of human PlgR is described. The recombinant domain I protein (rDI) was similar in structure to native SC domain I in that it bound specifically to MAb 6G11, an antibody which recognizes a critical portion of the PIg binding site in domain I. The biological activity of rDI was indicated by high affinity binding to PIgA (Kd = 1.6 × 10-7 M) and IgM (Kd = 5.1 × 10-7 M). Domain I of human SC is therefore sufficient for binding to PIg.

Original languageEnglish (US)
Pages (from-to)165-168
Number of pages4
JournalMolecular Immunology
Volume31
Issue number2
DOIs
StatePublished - 1994

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Polymeric Immunoglobulin Receptors
Immunoglobulin M
Peptide Fragments
Binding Sites
Escherichia coli
Ligands
Antibodies
Protein Domains

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Expression and purification of biologically active domain I of the human polymeric immunoglobulin receptor. / Bakos, Mary Ann; Widen, Steven; Goldblum, Randall M.

In: Molecular Immunology, Vol. 31, No. 2, 1994, p. 165-168.

Research output: Contribution to journalArticle

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