PubMed:9446624
Annnotations
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-57 | Sentence | denotes | Human small intestinal maltase-glucoamylase cDNA cloning. |
T2 | 58-89 | Sentence | denotes | Homology to sucrase-isomaltase. |
T3 | 90-157 | Sentence | denotes | It has been hypothesized that human mucosal glucoamylase (EC 3.2.1. |
T4 | 158-449 | Sentence | denotes | 20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. |
T5 | 450-719 | Sentence | denotes | As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. |
T6 | 720-803 | Sentence | denotes | Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. |
T7 | 804-970 | Sentence | denotes | Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. |
T8 | 971-1095 | Sentence | denotes | The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). |
T9 | 1096-1224 | Sentence | denotes | Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. |
T10 | 1225-1322 | Sentence | denotes | Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. |
T11 | 1323-1521 | Sentence | denotes | Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site. |
T1 | 0-57 | Sentence | denotes | Human small intestinal maltase-glucoamylase cDNA cloning. |
T2 | 58-89 | Sentence | denotes | Homology to sucrase-isomaltase. |
T3 | 90-157 | Sentence | denotes | It has been hypothesized that human mucosal glucoamylase (EC 3.2.1. |
T4 | 158-449 | Sentence | denotes | 20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. |
T5 | 450-719 | Sentence | denotes | As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. |
T6 | 720-803 | Sentence | denotes | Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. |
T7 | 804-970 | Sentence | denotes | Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. |
T8 | 971-1095 | Sentence | denotes | The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). |
T9 | 1096-1224 | Sentence | denotes | Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. |
T10 | 1225-1322 | Sentence | denotes | Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. |
T11 | 1323-1521 | Sentence | denotes | Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site. |
Glycosmos6-MAT
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 6-22 | http://purl.obolibrary.org/obo/MAT_0000047 | denotes | small intestinal |
T2 | 526-542 | http://purl.obolibrary.org/obo/MAT_0000047 | denotes | small intestinal |
T3 | 855-865 | http://purl.obolibrary.org/obo/MAT_0000043 | denotes | intestinal |
mondo_disease
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 307-319 | Disease | denotes | malnutrition | http://purl.obolibrary.org/obo/MONDO_0006873 |
Anatomy-MAT
Id | Subject | Object | Predicate | Lexical cue | mat_id |
---|---|---|---|---|---|
T1 | 6-22 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/MAT_0000047 |
T2 | 526-542 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/MAT_0000047 |
T3 | 855-865 | Body_part | denotes | intestinal | http://purl.obolibrary.org/obo/MAT_0000043 |
HP-phenotype
Id | Subject | Object | Predicate | Lexical cue | hp_id |
---|---|---|---|---|---|
T1 | 307-319 | Phenotype | denotes | malnutrition | HP:0004395 |
Glycan-GlyCosmos
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 635-642 | Glycan | denotes | maltose | https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT |
GlyCosmos15-HP
Id | Subject | Object | Predicate | Lexical cue | hp_id |
---|---|---|---|---|---|
T1 | 307-319 | Phenotype | denotes | malnutrition | HP:0004395 |
GlyCosmos15-MONDO
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 307-319 | Disease | denotes | malnutrition | http://purl.obolibrary.org/obo/MONDO_0006873 |
GlyCosmos15-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 0-5 | OrganismTaxon | denotes | Human | 9606 |
T2 | 120-125 | OrganismTaxon | denotes | human | 9606 |
T3 | 520-525 | OrganismTaxon | denotes | human | 9606 |
T4 | 720-725 | OrganismTaxon | denotes | Human | 9606 |
T5 | 849-854 | OrganismTaxon | denotes | human | 9606 |
GlyCosmos15-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 6-22 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/UBERON_0002108 |
T2 | 526-542 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/UBERON_0002108 |
GlyCosmos15-MAT
Id | Subject | Object | Predicate | Lexical cue | mat_id |
---|---|---|---|---|---|
T1 | 6-22 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/MAT_0000047 |
T2 | 526-542 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/MAT_0000047 |
T3 | 855-865 | Body_part | denotes | intestinal | http://purl.obolibrary.org/obo/MAT_0000043 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-57 | Sentence | denotes | Human small intestinal maltase-glucoamylase cDNA cloning. |
T2 | 58-89 | Sentence | denotes | Homology to sucrase-isomaltase. |
T3 | 90-157 | Sentence | denotes | It has been hypothesized that human mucosal glucoamylase (EC 3.2.1. |
T4 | 158-449 | Sentence | denotes | 20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. |
T5 | 450-719 | Sentence | denotes | As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. |
T6 | 720-803 | Sentence | denotes | Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. |
T7 | 804-970 | Sentence | denotes | Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. |
T8 | 971-1095 | Sentence | denotes | The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). |
T9 | 1096-1224 | Sentence | denotes | Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. |
T10 | 1225-1322 | Sentence | denotes | Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. |
T11 | 1323-1521 | Sentence | denotes | Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site. |
T1 | 0-57 | Sentence | denotes | Human small intestinal maltase-glucoamylase cDNA cloning. |
T2 | 58-89 | Sentence | denotes | Homology to sucrase-isomaltase. |
T3 | 90-157 | Sentence | denotes | It has been hypothesized that human mucosal glucoamylase (EC 3.2.1. |
T4 | 158-449 | Sentence | denotes | 20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. |
T5 | 450-719 | Sentence | denotes | As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. |
T6 | 720-803 | Sentence | denotes | Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. |
T7 | 804-970 | Sentence | denotes | Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. |
T8 | 971-1095 | Sentence | denotes | The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). |
T9 | 1096-1224 | Sentence | denotes | Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. |
T10 | 1225-1322 | Sentence | denotes | Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. |
T11 | 1323-1521 | Sentence | denotes | Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site. |
GlyCosmos15-Sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-57 | Sentence | denotes | Human small intestinal maltase-glucoamylase cDNA cloning. |
T2 | 58-89 | Sentence | denotes | Homology to sucrase-isomaltase. |
T3 | 90-157 | Sentence | denotes | It has been hypothesized that human mucosal glucoamylase (EC 3.2.1. |
T4 | 158-449 | Sentence | denotes | 20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. |
T5 | 450-719 | Sentence | denotes | As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. |
T6 | 720-803 | Sentence | denotes | Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. |
T7 | 804-970 | Sentence | denotes | Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. |
T8 | 971-1095 | Sentence | denotes | The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). |
T9 | 1096-1224 | Sentence | denotes | Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. |
T10 | 1225-1322 | Sentence | denotes | Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. |
T11 | 1323-1521 | Sentence | denotes | Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site. |
GlyCosmos15-Glycan
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 635-642 | Glycan | denotes | maltose | https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 0-5 | OrganismTaxon | denotes | Human | 9606 |
T2 | 120-125 | OrganismTaxon | denotes | human | 9606 |
T3 | 520-525 | OrganismTaxon | denotes | human | 9606 |
T4 | 720-725 | OrganismTaxon | denotes | Human | 9606 |
T5 | 849-854 | OrganismTaxon | denotes | human | 9606 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 6-22 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/UBERON_0002108 |
T2 | 526-542 | Body_part | denotes | small intestinal | http://purl.obolibrary.org/obo/UBERON_0002108 |