PubMed:2484027 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/2484027","sourcedb":"PubMed","sourceid":"2484027","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/2484027","text":"Substrate recognition by UDP-N-acetyl-alpha-D-galactosamine: polypeptide n-acetyl-alpha-D-galactosaminyltransferase. Effects of chain length and disulphide bonding of synthetic peptide substrates.\nA synthetic peptide AcTPPP, based on a threonine-containing sequence present in bovine myelin basic protein, is a potent acceptor of glycosyl transfer from UDP-N-acetylgalactosamine catalyzed by extracts of baby hamster kidney (BHK) cells or rabbit lymph node tissue. In contrast, the disulphide-linked peptide (AcTCPPP)2, based on a glycosylated sequence present in the hinge region of rabbit immunoglobulin G, is not an acceptor and inhibits glycosylation of AcTPPP. Extension of the cystine-containing peptide at the N-terminus produced weak acceptors but strong acceptors resulted when the cystine residue was reduced to form monomeric peptides. The acceptor specificity of the N-acetylgalactosaminyl-transferase activity of BHK cells is very similar to that of rabbit lymph node tissue. The results indicated that tissues actively secreting immunoglobulin do not contain a transferase activity adapted specifically for glycosylation of sequences containing cystine residues, and suggested that addition of an N-acetylgalactosamine to a threonine residue in the hinge region of rabbit immunoglobulin takes place during biosynthesis prior to the formation of the inter-chain disulphide bridge of fully assembled 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