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Intracellular targetting signals of polymeric immunoglobulin receptors are highly conserved between species
Author(s) -
Banting George,
Brake Brigitte,
Braghetta Paola,
Luzio J.Paul,
Stanley Keith K.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81034-8
Subject(s) - polyclonal antibodies , complementary dna , biology , microbiology and biotechnology , peptide sequence , antiserum , polymeric immunoglobulin receptor , homology (biology) , amino acid , receptor , antibody , immunoglobulin domain , golgi apparatus , gene , biochemistry , genetics , cell
A rat liver cDNA library, constructed in the plasmid expression vector pUEX, was immunoscreened using a rabbit polyclonal antiserum raised against rat liver Golgi membrane proteins. A sub‐set of isolated clones were shown to encode the rat polymeric immunoglobulin receptor (pIgR). DNA sequence analysis of these clones provided the complete coding sequence of rat pIgR. Subsequent alignment of rat, rabbit and human predicted amino acid sequences demonstrated that the greatest degree of homology between the three pIgRs lies in their cytoplasmic tails; a region previously shown to be important for correct targetting and trancytosis of rabbit pIgR [(1984) Nature 308, 37–43].