PubMed:12039536 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":126,"end":225},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":226,"end":363},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":364,"end":417},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":418,"end":593},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":363},"obj":"Sentence"},{"id":"T4","span":{"begin":364,"end":417},"obj":"Sentence"},{"id":"T5","span":{"begin":418,"end":593},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant alpha-(1--\u003e4)-galactosyltransferase.\nA truncated alpha-(1--\u003e4)-galactosyltransferase (LgtC) gene from Neisseria meningitidis was cloned. The recombinant glycosyltransferase was expressed in Escherichia coli BL21 (DE3) strain with high specific activity (5 units/mg protein). Its acceptor specificity was carefully characterized. Then the purified enzyme was utilized in highly efficient syntheses of globotriose and a variety of alpha-(1--\u003e4)-galactosylated derivatives as potential antibacterial agents."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":191,"end":213},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":279,"end":295},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"487"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"}],"text":"Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant alpha-(1--\u003e4)-galactosyltransferase.\nA truncated alpha-(1--\u003e4)-galactosyltransferase (LgtC) gene from Neisseria meningitidis was cloned. The recombinant glycosyltransferase was expressed in Escherichia coli BL21 (DE3) strain with high specific activity (5 units/mg protein). Its acceptor specificity was carefully characterized. Then the purified enzyme was utilized in highly efficient syntheses of globotriose and a variety of alpha-(1--\u003e4)-galactosylated derivatives as potential antibacterial agents."}