PubMed:2950996 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":115,"end":314},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":315,"end":391},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":392,"end":555},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":556,"end":699},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":700,"end":892},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":314},"obj":"Sentence"},{"id":"T3","span":{"begin":315,"end":391},"obj":"Sentence"},{"id":"T4","span":{"begin":392,"end":555},"obj":"Sentence"},{"id":"T5","span":{"begin":556,"end":699},"obj":"Sentence"},{"id":"T6","span":{"begin":700,"end":892},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.\nA simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":283,"end":287},"obj":"HP_0000365"}],"text":"Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.\nA simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":93,"end":113},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":224,"end":244},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1309"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1309"}],"text":"Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.\nA simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":41,"end":54},"obj":"Body_part"},{"id":"T2","span":{"begin":155,"end":168},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005576"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005576"}],"text":"Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.\nA simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans."}