PubMed:3242801 JSONTXT

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    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":105,"end":287},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":288,"end":412},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":413,"end":763},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":764,"end":884},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}

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