The amino-terminal domain of rabbit secretory component is responsible for noncovalent binding to immunoglobulin A dimers.

This publication has 37 references indexed in Scilit:

• The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains
  Nature, 1984
• Biosynthesis of the iga antibody receptor: A model for the transepithelial sorting of a membrane glycoprotein
  Cell, 1984
• MONOCLONAL ANTIBODIES RECOGNIZING THE SECRETED AND MEMBRANE DOMAINS OF THE IgA DIMER RECEPTOR*
  Annals of the New York Academy of Sciences, 1983
• Human secretory component—VI: Immunoglobulin-binding properties
  Immunochemistry, 1977
• N-terminal sequences of secretory piece and of α chains of different allotype in rabbit secretory IgA
  Nature, 1975
• Gross Conformation of Human Secretory Immunoglobulin A and Its Component Parts
  European Journal of Biochemistry, 1974
• Studies on human secretory IgA (II). Comparative studies on a fragment of secretory component derived from secretory IgA and fragments obtained by enzymatic digestion of free secretory component
  Immunochemistry, 1973
• Rabbit immunoglobulin A allotypic specificities. Localization to two papain fragments, Fab2.alpha. and Fc2.alpha., of secretory immunoglobulin A
  Biochemistry, 1973
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• CHARACTERISTICS OF AN IMMUNE SYSTEM COMMON TO CERTAIN EXTERNAL SECRETIONS
  The Journal of Experimental Medicine, 1965