PubMed:8394350 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":212},"obj":"Sentence"},{"id":"T3","span":{"begin":213,"end":344},"obj":"Sentence"},{"id":"T4","span":{"begin":345,"end":441},"obj":"Sentence"},{"id":"T5","span":{"begin":442,"end":551},"obj":"Sentence"},{"id":"T6","span":{"begin":552,"end":657},"obj":"Sentence"},{"id":"T7","span":{"begin":658,"end":861},"obj":"Sentence"},{"id":"T8","span":{"begin":862,"end":947},"obj":"Sentence"},{"id":"T9","span":{"begin":948,"end":1023},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":113},"obj":"Sentence"},{"id":"T2","span":{"begin":114,"end":212},"obj":"Sentence"},{"id":"T3","span":{"begin":213,"end":344},"obj":"Sentence"},{"id":"T4","span":{"begin":345,"end":441},"obj":"Sentence"},{"id":"T5","span":{"begin":442,"end":551},"obj":"Sentence"},{"id":"T6","span":{"begin":552,"end":657},"obj":"Sentence"},{"id":"T7","span":{"begin":658,"end":861},"obj":"Sentence"},{"id":"T8","span":{"begin":862,"end":947},"obj":"Sentence"},{"id":"T9","span":{"begin":948,"end":1023},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.\nA protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":195,"end":211},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"562"}],"text":"Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.\nA protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":167,"end":173},"obj":"Body_part"},{"id":"T2","span":{"begin":644,"end":650},"obj":"Body_part"},{"id":"T3","span":{"begin":662,"end":668},"obj":"Body_part"},{"id":"T4","span":{"begin":790,"end":796},"obj":"Body_part"},{"id":"T5","span":{"begin":906,"end":912},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0013424"}],"text":"Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.\nA protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation."}