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Post‐translational modification of the β‐subunit of the human fibronectin receptor
Author(s) -
Jaspers Martine,
de Strooper Bart,
Spaepen Marijke,
van Leuven Fred,
David Guido,
van den Berghe Herman,
Cassiman Jean-Jacques
Publication year - 1988
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(88)80859-7
Subject(s) - protein subunit , fibronectin , posttranslational modification , chemistry , receptor , microbiology and biotechnology , biophysics , biochemistry , biology , gene , enzyme , extracellular matrix
Monoclonal antibody DH12, directed against the β‐subunit of the fibronectin receptor recognizes a doublet of proteins (100 and 110 kDa) in Western blots of solubilized whole fibroblasts. Pulse‐chase experiments with [ 35 S]methionine in human skin fibroblasts suggested that the two proteins might be metabolically related as precursor (100 kDa) and product (110 kDa). Endo H digestion and [ 3 H]fucose labeling suggested that maturation converted the high‐mannose oligosaccharides (100 kDa) to the endoglycosidase H resistant complex type (110 kDa). This was supported by N ‐glycanase digestion and by chemical deglycosylation which showed a single polypeptide. Surface iodination of intact cells labeled only the presumed mature β‐subunit.