> top > docs > PubMed:6435871 > annotations

PubMed:6435871 JSONTXT

Annnotations TAB JSON ListView MergeView

CL-cell

Id Subject Object Predicate Lexical cue cl_id
T1 688-705 Cell denotes fractionated on a http://purl.obolibrary.org/obo/CL:0002045

sentences

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-139 Sentence denotes Structure studies of amylose-V complexes and retrograded amylose by action of alpha amylases, and a new method for preparing amylodextrins.
TextSentencer_T2 140-379 Sentence denotes Human-salivary, porcine-pancreatic, and Bacillus subtilis alpha amylases were used to study the structure of amylose-V complexes with butyl alcohol, tert-butyl alcohol, 1,1,2,2-tetrachloroethane, and 1-naphthol, and of retrograded amylose.
TextSentencer_T3 380-540 Sentence denotes Alpha amylase hydrolyzes the amorphous, folding areas on the surfaces of the lamella of packed helices, with the formation of resistant, amylodextrin fragments.
TextSentencer_T4 541-658 Sentence denotes Their degree of polymerization (d.p.) corresponds to the diameter of the helices and the folding length of the chain.
TextSentencer_T5 659-731 Sentence denotes The resistant fragments were fractionated on a column of Bio-Gel A-0.5m.
TextSentencer_T6 732-1139 Sentence denotes Gel filtration of human-salivary and porcine-pancreatic alpha amylase hydrolyzates gave resistant fragments whose peak fractions, i.e., the three pooled fractions from the gel-filtration column with the highest amount of carbohydrate, had a d.p. of 75 +/- 4 for the amylose complex with butyl alcohol, 90 +/- 3 for those with tert-butyl alcohol and tetrachloroethane, and 123 +/- 2 for that with 1-naphthol.
TextSentencer_T7 1140-1425 Sentence denotes These d.p. values correspond to helices of six residues per turn with a folding length of 10 nm, seven residues per turn with a folding length of 10 nm, and eight residues per turn with a folding length of 12 nm (or nine residues per turn with a folding length of 10 nm), respectively.
TextSentencer_T8 1426-1607 Sentence denotes Acid hydrolysis of retrograded amylose gave a resistant fragment having an average d.p. of 32, human-salivary and porcine-pancreatic alpha amylases gave a resistant fragment of d.p.
TextSentencer_T9 1608-1681 Sentence denotes 43, and Bacillus subtilis alpha amylase gave a resistant fragment of d.p.
TextSentencer_T10 1682-1685 Sentence denotes 50.
TextSentencer_T11 1686-1846 Sentence denotes A structure for retrograded amylose is proposed in which there are crystalline, double-helical regions that are 10 nm long, interspersed with amorphous regions.
TextSentencer_T12 1847-1954 Sentence denotes The amorphous regions are hydrolyzed by acid and by alpha amylases, leaving the crystalline regions intact.
TextSentencer_T13 1955-2444 Sentence denotes The differences in the sizes of the resistant amylodextrins depend on the differences in the specificities of the hydrolyzing agents: acid hydrolyzes right up to the edge of the crystalline region, whereas the alpha amylases hydrolyze up to some point several D-glucosyl residues away from the crystalline region, leaving "stubs" on the ends of the amylodextrins whose sizes are dependent on the sizes of the binding sites of the individual alpha amylases.(ABSTRACT TRUNCATED AT 400 WORDS)
T1 0-139 Sentence denotes Structure studies of amylose-V complexes and retrograded amylose by action of alpha amylases, and a new method for preparing amylodextrins.
T2 140-379 Sentence denotes Human-salivary, porcine-pancreatic, and Bacillus subtilis alpha amylases were used to study the structure of amylose-V complexes with butyl alcohol, tert-butyl alcohol, 1,1,2,2-tetrachloroethane, and 1-naphthol, and of retrograded amylose.
T3 380-540 Sentence denotes Alpha amylase hydrolyzes the amorphous, folding areas on the surfaces of the lamella of packed helices, with the formation of resistant, amylodextrin fragments.
T4 541-658 Sentence denotes Their degree of polymerization (d.p.) corresponds to the diameter of the helices and the folding length of the chain.
T5 659-731 Sentence denotes The resistant fragments were fractionated on a column of Bio-Gel A-0.5m.
T6 732-1139 Sentence denotes Gel filtration of human-salivary and porcine-pancreatic alpha amylase hydrolyzates gave resistant fragments whose peak fractions, i.e., the three pooled fractions from the gel-filtration column with the highest amount of carbohydrate, had a d.p. of 75 +/- 4 for the amylose complex with butyl alcohol, 90 +/- 3 for those with tert-butyl alcohol and tetrachloroethane, and 123 +/- 2 for that with 1-naphthol.
T7 1140-1425 Sentence denotes These d.p. values correspond to helices of six residues per turn with a folding length of 10 nm, seven residues per turn with a folding length of 10 nm, and eight residues per turn with a folding length of 12 nm (or nine residues per turn with a folding length of 10 nm), respectively.
T8 1426-1607 Sentence denotes Acid hydrolysis of retrograded amylose gave a resistant fragment having an average d.p. of 32, human-salivary and porcine-pancreatic alpha amylases gave a resistant fragment of d.p.
T9 1608-1681 Sentence denotes 43, and Bacillus subtilis alpha amylase gave a resistant fragment of d.p.
T10 1682-1685 Sentence denotes 50.
T11 1686-1846 Sentence denotes A structure for retrograded amylose is proposed in which there are crystalline, double-helical regions that are 10 nm long, interspersed with amorphous regions.
T12 1847-1954 Sentence denotes The amorphous regions are hydrolyzed by acid and by alpha amylases, leaving the crystalline regions intact.
T13 1955-2444 Sentence denotes The differences in the sizes of the resistant amylodextrins depend on the differences in the specificities of the hydrolyzing agents: acid hydrolyzes right up to the edge of the crystalline region, whereas the alpha amylases hydrolyze up to some point several D-glucosyl residues away from the crystalline region, leaving "stubs" on the ends of the amylodextrins whose sizes are dependent on the sizes of the binding sites of the individual alpha amylases.(ABSTRACT TRUNCATED AT 400 WORDS)

GlyCosmos15-Glycan

Id Subject Object Predicate Lexical cue image
T1 21-28 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T2 57-64 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T3 249-256 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T4 371-378 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T5 998-1005 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T6 1457-1464 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T7 1714-1721 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL

Glycan-GlyCosmos

Id Subject Object Predicate Lexical cue image
T1 21-28 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T2 57-64 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T3 249-256 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T4 371-378 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T5 998-1005 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T6 1457-1464 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL
T7 1714-1721 Glycan denotes amylose https://api.glycosmos.org/wurcs2image/latest/png/binary/G05740LL

GlyCosmos15-CL

Id Subject Object Predicate Lexical cue cl_id
T1 688-705 Cell denotes fractionated on a http://purl.obolibrary.org/obo/CL:0002045

GlyCosmos15-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 457-464 Body_part denotes lamella http://purl.obolibrary.org/obo/UBERON_0004529

GlyCosmos15-Taxon

Id Subject Object Predicate Lexical cue db_id
T1 140-145 Organism denotes Human 9606
T2 180-197 Organism denotes Bacillus subtilis 1423
T3 457-464 Organism denotes lamella 1408216
T4 750-755 Organism denotes human 9606
T5 1521-1526 Organism denotes human 9606
T6 1616-1633 Organism denotes Bacillus subtilis 1423

GlyCosmos15-Sentences

Id Subject Object Predicate Lexical cue
T1 0-139 Sentence denotes Structure studies of amylose-V complexes and retrograded amylose by action of alpha amylases, and a new method for preparing amylodextrins.
T2 140-379 Sentence denotes Human-salivary, porcine-pancreatic, and Bacillus subtilis alpha amylases were used to study the structure of amylose-V complexes with butyl alcohol, tert-butyl alcohol, 1,1,2,2-tetrachloroethane, and 1-naphthol, and of retrograded amylose.
T3 380-540 Sentence denotes Alpha amylase hydrolyzes the amorphous, folding areas on the surfaces of the lamella of packed helices, with the formation of resistant, amylodextrin fragments.
T4 541-658 Sentence denotes Their degree of polymerization (d.p.) corresponds to the diameter of the helices and the folding length of the chain.
T5 659-731 Sentence denotes The resistant fragments were fractionated on a column of Bio-Gel A-0.5m.
T6 732-1139 Sentence denotes Gel filtration of human-salivary and porcine-pancreatic alpha amylase hydrolyzates gave resistant fragments whose peak fractions, i.e., the three pooled fractions from the gel-filtration column with the highest amount of carbohydrate, had a d.p. of 75 +/- 4 for the amylose complex with butyl alcohol, 90 +/- 3 for those with tert-butyl alcohol and tetrachloroethane, and 123 +/- 2 for that with 1-naphthol.
T7 1140-1425 Sentence denotes These d.p. values correspond to helices of six residues per turn with a folding length of 10 nm, seven residues per turn with a folding length of 10 nm, and eight residues per turn with a folding length of 12 nm (or nine residues per turn with a folding length of 10 nm), respectively.
T8 1426-1607 Sentence denotes Acid hydrolysis of retrograded amylose gave a resistant fragment having an average d.p. of 32, human-salivary and porcine-pancreatic alpha amylases gave a resistant fragment of d.p.
T9 1608-1681 Sentence denotes 43, and Bacillus subtilis alpha amylase gave a resistant fragment of d.p.
T10 1682-1685 Sentence denotes 50.
T11 1686-1846 Sentence denotes A structure for retrograded amylose is proposed in which there are crystalline, double-helical regions that are 10 nm long, interspersed with amorphous regions.
T12 1847-1954 Sentence denotes The amorphous regions are hydrolyzed by acid and by alpha amylases, leaving the crystalline regions intact.
T13 1955-2444 Sentence denotes The differences in the sizes of the resistant amylodextrins depend on the differences in the specificities of the hydrolyzing agents: acid hydrolyzes right up to the edge of the crystalline region, whereas the alpha amylases hydrolyze up to some point several D-glucosyl residues away from the crystalline region, leaving "stubs" on the ends of the amylodextrins whose sizes are dependent on the sizes of the binding sites of the individual alpha amylases.(ABSTRACT TRUNCATED AT 400 WORDS)

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 140-145 OrganismTaxon denotes Human 9606
T2 180-197 OrganismTaxon denotes Bacillus subtilis 1423
T3 457-464 OrganismTaxon denotes lamella 1408216
T4 750-755 OrganismTaxon denotes human 9606
T5 1521-1526 OrganismTaxon denotes human 9606
T6 1616-1633 OrganismTaxon denotes Bacillus subtilis 1423

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 457-464 Body_part denotes lamella http://purl.obolibrary.org/obo/UBERON_0004529