PubMed:9446624 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":57},"obj":"Sentence"},{"id":"T2","span":{"begin":58,"end":89},"obj":"Sentence"},{"id":"T3","span":{"begin":90,"end":157},"obj":"Sentence"},{"id":"T4","span":{"begin":158,"end":449},"obj":"Sentence"},{"id":"T5","span":{"begin":450,"end":719},"obj":"Sentence"},{"id":"T6","span":{"begin":720,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1224},"obj":"Sentence"},{"id":"T10","span":{"begin":1225,"end":1322},"obj":"Sentence"},{"id":"T11","span":{"begin":1323,"end":1521},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":57},"obj":"Sentence"},{"id":"T2","span":{"begin":58,"end":89},"obj":"Sentence"},{"id":"T3","span":{"begin":90,"end":157},"obj":"Sentence"},{"id":"T4","span":{"begin":158,"end":449},"obj":"Sentence"},{"id":"T5","span":{"begin":450,"end":719},"obj":"Sentence"},{"id":"T6","span":{"begin":720,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1224},"obj":"Sentence"},{"id":"T10","span":{"begin":1225,"end":1322},"obj":"Sentence"},{"id":"T11","span":{"begin":1323,"end":1521},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":6,"end":22},"obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"T2","span":{"begin":526,"end":542},"obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"T3","span":{"begin":855,"end":865},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":307,"end":319},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0006873"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":6,"end":22},"obj":"Body_part"},{"id":"T2","span":{"begin":526,"end":542},"obj":"Body_part"},{"id":"T3","span":{"begin":855,"end":865},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":307,"end":319},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0004395"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":635,"end":642},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":307,"end":319},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0004395"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":307,"end":319},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0006873"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":120,"end":125},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":520,"end":525},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":720,"end":725},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":849,"end":854},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":6,"end":22},"obj":"Body_part"},{"id":"T2","span":{"begin":526,"end":542},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":6,"end":22},"obj":"Body_part"},{"id":"T2","span":{"begin":526,"end":542},"obj":"Body_part"},{"id":"T3","span":{"begin":855,"end":865},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":57},"obj":"Sentence"},{"id":"T2","span":{"begin":58,"end":89},"obj":"Sentence"},{"id":"T3","span":{"begin":90,"end":157},"obj":"Sentence"},{"id":"T4","span":{"begin":158,"end":449},"obj":"Sentence"},{"id":"T5","span":{"begin":450,"end":719},"obj":"Sentence"},{"id":"T6","span":{"begin":720,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1224},"obj":"Sentence"},{"id":"T10","span":{"begin":1225,"end":1322},"obj":"Sentence"},{"id":"T11","span":{"begin":1323,"end":1521},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":57},"obj":"Sentence"},{"id":"T2","span":{"begin":58,"end":89},"obj":"Sentence"},{"id":"T3","span":{"begin":90,"end":157},"obj":"Sentence"},{"id":"T4","span":{"begin":158,"end":449},"obj":"Sentence"},{"id":"T5","span":{"begin":450,"end":719},"obj":"Sentence"},{"id":"T6","span":{"begin":720,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1224},"obj":"Sentence"},{"id":"T10","span":{"begin":1225,"end":1322},"obj":"Sentence"},{"id":"T11","span":{"begin":1323,"end":1521},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":57},"obj":"Sentence"},{"id":"T2","span":{"begin":58,"end":89},"obj":"Sentence"},{"id":"T3","span":{"begin":90,"end":157},"obj":"Sentence"},{"id":"T4","span":{"begin":158,"end":449},"obj":"Sentence"},{"id":"T5","span":{"begin":450,"end":719},"obj":"Sentence"},{"id":"T6","span":{"begin":720,"end":803},"obj":"Sentence"},{"id":"T7","span":{"begin":804,"end":970},"obj":"Sentence"},{"id":"T8","span":{"begin":971,"end":1095},"obj":"Sentence"},{"id":"T9","span":{"begin":1096,"end":1224},"obj":"Sentence"},{"id":"T10","span":{"begin":1225,"end":1322},"obj":"Sentence"},{"id":"T11","span":{"begin":1323,"end":1521},"obj":"Sentence"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":635,"end":642},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":120,"end":125},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":520,"end":525},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":720,"end":725},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":849,"end":854},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":6,"end":22},"obj":"Body_part"},{"id":"T2","span":{"begin":526,"end":542},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"}],"text":"Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.\nIt has been hypothesized that human mucosal glucoamylase (EC 3.2.1. 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. 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. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. 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."}