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J. Biol. Chem., Vol. 263, Issue 28, 14211-14215, 10, 1988
AF Purchio, JA Cooper, AM Brunner, MN Lioubin, LE Gentry, KS Kovacina, RA Roth and H Marquardt
Oncogen, Seattle, Washington 98121.
Recombinant transforming growth factor-beta 1 (TGF-beta 1) precursor produced and secreted by a clone of Chinese hamster ovary cells was found to be glycosylated and phosphorylated. Treatment of 32P-labeled precursor protein with N-glycanase indicated that phosphate was incorporated into asparagine-linked complex carbohydrate moieties. Fractionation of 32P-labeled glycopeptides followed by amino acid sequence analysis indicated that greater than 95% of the label was incorporated into two out of three glycosylation sites at Asn-82 and Asn-136 of the TGF-beta 1 precursor. Two-dimensional electrophoretic analysis of acid hydrolyzed precursor protein and precursor protein- derived glycopeptides indicated that 32P was incorporated as mannose 6- phosphate. Binding studies with the purified receptor for mannose 6- phosphate indicated that the TGF-beta 1 precursor could bind to this receptor and the binding was specifically inhibited with mannose 6- phosphate.
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