Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-beta 1 precursor.

作者: A F Purchio , J A Cooper , A M Brunner , M N Lioubin , L E Gentry

DOI: 10.1016/S0021-9258(18)68207-9

关键词:

摘要: 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 phosphorylated. Treatment 32P-labeled protein with N-glycanase indicated that phosphate incorporated into asparagine-linked complex carbohydrate moieties. Fractionation glycopeptides followed amino acid sequence analysis greater than 95% the label two out three glycosylation sites at Asn-82 Asn-136 TGF-beta precursor. Two-dimensional electrophoretic hydrolyzed protein-derived 32P as mannose 6-phosphate. Binding studies purified receptor for 6-phosphate could bind this binding specifically inhibited

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