| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-116 |
Sentence |
denotes |
Substrate recognition by UDP-N-acetyl-alpha-D-galactosamine: polypeptide n-acetyl-alpha-D-galactosaminyltransferase. |
| T1 |
0-116 |
Sentence |
denotes |
Substrate recognition by UDP-N-acetyl-alpha-D-galactosamine: polypeptide n-acetyl-alpha-D-galactosaminyltransferase. |
| TextSentencer_T2 |
117-196 |
Sentence |
denotes |
Effects of chain length and disulphide bonding of synthetic peptide substrates. |
| T2 |
117-196 |
Sentence |
denotes |
Effects of chain length and disulphide bonding of synthetic peptide substrates. |
| TextSentencer_T3 |
197-464 |
Sentence |
denotes |
A 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. |
| T3 |
197-464 |
Sentence |
denotes |
A 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. |
| TextSentencer_T4 |
465-665 |
Sentence |
denotes |
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. |
| T4 |
465-665 |
Sentence |
denotes |
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. |
| TextSentencer_T5 |
666-846 |
Sentence |
denotes |
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. |
| T5 |
666-846 |
Sentence |
denotes |
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. |
| TextSentencer_T6 |
847-988 |
Sentence |
denotes |
The acceptor specificity of the N-acetylgalactosaminyl-transferase activity of BHK cells is very similar to that of rabbit lymph node tissue. |
| T6 |
847-988 |
Sentence |
denotes |
The acceptor specificity of the N-acetylgalactosaminyl-transferase activity of BHK cells is very similar to that of rabbit lymph node tissue. |
| TextSentencer_T7 |
989-1428 |
Sentence |
denotes |
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 immunoglobulins. |
| T7 |
989-1428 |
Sentence |
denotes |
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 immunoglobulins. |
