PubMed:16694 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":60},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":61,"end":300},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":301,"end":415},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":416,"end":522},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":523,"end":619},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":620,"end":700},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":60},"obj":"Sentence"},{"id":"T2","span":{"begin":61,"end":300},"obj":"Sentence"},{"id":"T3","span":{"begin":301,"end":415},"obj":"Sentence"},{"id":"T4","span":{"begin":416,"end":522},"obj":"Sentence"},{"id":"T5","span":{"begin":523,"end":619},"obj":"Sentence"},{"id":"T6","span":{"begin":620,"end":700},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"An endo-(1 leads to 3)-beta-D-glucanase from Mucor hiemalis.\nAn endo-(1 leads to 3)-beta-D-glucanase (EC 3.2.1.6), isolated from the culture filtrate of the fungus Mucor hiemalis, was purified by ammonium sulfate fractionation, gel filtration, and column chromatography on O-(carboxymethyl)cellulose. The optimum pH, optimum temperature, and Km value of the enzyme were pH 5.0, 50 degrees, and 0.048%, respectively. The enzyme was strongly inactivated by Pb2+, Cu2+, and Hg2+ ions and also inhibited by Zn2+ and Fe3+ ions. The enzyme was specific for laminaran and the action pattern of the enzyme was of the endo-type. The molecular weight of the enzyme, as determined by gel filtration, was 30,000."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":164,"end":178},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"64493"},{"id":"A2","pred":"db_id","subj":"T2","obj":"64493"}],"text":"An endo-(1 leads to 3)-beta-D-glucanase from Mucor hiemalis.\nAn endo-(1 leads to 3)-beta-D-glucanase (EC 3.2.1.6), isolated from the culture filtrate of the fungus Mucor hiemalis, was purified by ammonium sulfate fractionation, gel filtration, and column chromatography on O-(carboxymethyl)cellulose. The optimum pH, optimum temperature, and Km value of the enzyme were pH 5.0, 50 degrees, and 0.048%, respectively. The enzyme was strongly inactivated by Pb2+, Cu2+, and Hg2+ ions and also inhibited by Zn2+ and Fe3+ ions. The enzyme was specific for laminaran and the action pattern of the enzyme was of the endo-type. The molecular weight of the enzyme, as determined by gel filtration, was 30,000."}