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PubMed:3877569 JSONTXT

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GlyCosmos6-Glycan-Motif-Image

Id Subject Object Predicate Lexical cue image
T1 985-992 Glycan_Motif denotes glucose https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG

GlyCosmos6-Glycan-Motif-Structure

Id Subject Object Predicate Lexical cue
T1 985-992 https://glytoucan.org/Structures/Glycans/G15021LG denotes glucose

sentences

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-145 Sentence denotes The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues.
TextSentencer_T2 146-273 Sentence denotes A modified amylose containing 10% of tritiated D-allose residues has been hydrolyzed by porcine pancreatic alpha amylase (PPA).
TextSentencer_T3 274-442 Sentence denotes This reaction produced a number of radioactive oligosaccharides of low molecular weight, including modified mono-, di-, and tri-saccharides, as well as larger products.
TextSentencer_T4 443-592 Sentence denotes Analysis of these products by chemical and enzymic methods identified D-allose, two isomers of modified maltose, and isomers of modified maltotriose.
TextSentencer_T5 593-772 Sentence denotes These results may be interpreted in terms of current PPA models to indicate that D-allose residues may be productively bound at all five subsites of the active site of the enzyme.
TextSentencer_T6 773-993 Sentence denotes The distribution of modified residues in these products, however, further suggests that productive binding of D-allose at the subsite where catalytic attack occurs (subsite 3) is less favorable than binding of D-glucose.
TextSentencer_T7 994-1115 Sentence denotes These results are compared with results of a series of PPA substrates having modifications at C-3 and at other positions.
TextSentencer_T8 1116-1331 Sentence denotes Trends observed in enzyme hydrolysis of these modified substrates reflect factors that contribute to PPA catalysis, with respect to steric, electronic, and hydrogen-bonding interactions between enzyme and substrate.
T1 0-145 Sentence denotes The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues.
T2 146-273 Sentence denotes A modified amylose containing 10% of tritiated D-allose residues has been hydrolyzed by porcine pancreatic alpha amylase (PPA).
T3 274-442 Sentence denotes This reaction produced a number of radioactive oligosaccharides of low molecular weight, including modified mono-, di-, and tri-saccharides, as well as larger products.
T4 443-592 Sentence denotes Analysis of these products by chemical and enzymic methods identified D-allose, two isomers of modified maltose, and isomers of modified maltotriose.
T5 593-772 Sentence denotes These results may be interpreted in terms of current PPA models to indicate that D-allose residues may be productively bound at all five subsites of the active site of the enzyme.
T6 773-993 Sentence denotes The distribution of modified residues in these products, however, further suggests that productive binding of D-allose at the subsite where catalytic attack occurs (subsite 3) is less favorable than binding of D-glucose.
T7 994-1115 Sentence denotes These results are compared with results of a series of PPA substrates having modifications at C-3 and at other positions.
T8 1116-1331 Sentence denotes Trends observed in enzyme hydrolysis of these modified substrates reflect factors that contribute to PPA catalysis, with respect to steric, electronic, and hydrogen-bonding interactions between enzyme and substrate.

GlyCosmos15-Glycan

Id Subject Object Predicate Lexical cue image
T1 108-115 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T2 157-164 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T3 547-554 Glycan denotes maltose https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT

mondo_disease

Id Subject Object Predicate Lexical cue mondo_id
T1 268-271 Disease denotes PPA http://purl.obolibrary.org/obo/MONDO_0019806
T2 646-649 Disease denotes PPA http://purl.obolibrary.org/obo/MONDO_0019806
T3 1049-1052 Disease denotes PPA http://purl.obolibrary.org/obo/MONDO_0019806
T4 1217-1220 Disease denotes PPA http://purl.obolibrary.org/obo/MONDO_0019806

Glycan-GlyCosmos

Id Subject Object Predicate Lexical cue image
T1 108-115 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T2 157-164 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T3 547-554 Glycan denotes maltose https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT

GlyCosmos15-Sentences

Id Subject Object Predicate Lexical cue
T1 0-145 Sentence denotes The effect of substrate modification on binding of porcine pancreatic alpha amylase: hydrolysis of modified amylose containing D-allose residues.
T2 146-273 Sentence denotes A modified amylose containing 10% of tritiated D-allose residues has been hydrolyzed by porcine pancreatic alpha amylase (PPA).
T3 274-442 Sentence denotes This reaction produced a number of radioactive oligosaccharides of low molecular weight, including modified mono-, di-, and tri-saccharides, as well as larger products.
T4 443-592 Sentence denotes Analysis of these products by chemical and enzymic methods identified D-allose, two isomers of modified maltose, and isomers of modified maltotriose.
T5 593-772 Sentence denotes These results may be interpreted in terms of current PPA models to indicate that D-allose residues may be productively bound at all five subsites of the active site of the enzyme.
T6 773-993 Sentence denotes The distribution of modified residues in these products, however, further suggests that productive binding of D-allose at the subsite where catalytic attack occurs (subsite 3) is less favorable than binding of D-glucose.
T7 994-1115 Sentence denotes These results are compared with results of a series of PPA substrates having modifications at C-3 and at other positions.
T8 1116-1331 Sentence denotes Trends observed in enzyme hydrolysis of these modified substrates reflect factors that contribute to PPA catalysis, with respect to steric, electronic, and hydrogen-bonding interactions between enzyme and substrate.