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In vitro biosynthesis of the human cell surface receptor for transferrin
Author(s) -
Schneider C.,
Asser U.,
Sutherland D.R.,
Greaves M.F.
Publication year - 1983
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(83)80591-2
Subject(s) - reticulocyte , tunicamycin , transferrin receptor , polyclonal antibodies , in vitro , transferrin , receptor , glycosylation , cell surface receptor , transmembrane protein , biochemistry , biology , microbiology and biotechnology , cell , chemistry , antibody , endoplasmic reticulum , rna , gene , unfolded protein response , immunology
The human cell surface receptor for transferrin is a transmembrane phosphoglycoprotein composed of two disulphide linked and apparently identical subunits of M r 90 000. Using an affinity purified, polyclonal rabbit antibody, we have studied the in vitro biosynthesis of this receptor. The primary translation product, synthesised in a rabbit reticulocyte lysate programmed with human placental RNA, appears to have the same M r (78 000) as the unglycosylated molecule immunoprecipitated from tunicamycin‐treated cells. In the presence of a dog pancreatic microsomal system the cell free system accurately reproduces the glycosylation and the asymmetric transmembrane integration