PubMed:2136349 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":13,"end":32},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":559,"end":578},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":760,"end":779},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1002,"end":1011},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1012,"end":1033},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G27025MB"}],"text":"Synthesis of N-acetylglucosamine derivatives as probes for specificity of chicken hepatic lectin.\nSyntheses of the following compounds are described: 6-(Trifluoroacetylamino)hexyl 2-acetamido-2,6-dideoxy-beta-D-glucopyranoside and 2-acetamido-2-deoxy-alpha-D-xylopyranoside, two allyl 2-acetamido-2-deoxy-alpha-D-glucopyranosiduronic acid derivatives, and several allyl 2-acylamido-2-deoxy-beta-D-glucopyranosides having different acyl groups. These and other compounds were used as inhibitors in the binding assay for the chicken hepatic lectin specific for N-acetylglucosamine. We found that: 1) The inhibitory potency of N-acylglucosamine derivatives decreased progressively with increase in the size of acyl group, 2) absence of either 3- or 4-OH group of N-acetylglucosamine lowered the binding affinity more than 100-fold, and 3) the presence of a negatively charged group (carboxylic acid) at the C-6 position did not lower the affinity. The first two items are similar to the mammalian hepatic galactose/N-acetylgalactosamine lectins, but the last item is in a strong contrast to the mammalian lectins."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":97},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":98,"end":149},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":150,"end":443},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":444,"end":579},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":580,"end":594},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":595,"end":944},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":945,"end":1110},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":97},"obj":"Sentence"},{"id":"T2","span":{"begin":98,"end":149},"obj":"Sentence"},{"id":"T3","span":{"begin":150,"end":443},"obj":"Sentence"},{"id":"T4","span":{"begin":444,"end":579},"obj":"Sentence"},{"id":"T5","span":{"begin":580,"end":594},"obj":"Sentence"},{"id":"T6","span":{"begin":595,"end":944},"obj":"Sentence"},{"id":"T7","span":{"begin":945,"end":1110},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Synthesis of N-acetylglucosamine derivatives as probes for specificity of chicken hepatic lectin.\nSyntheses of the following compounds are described: 6-(Trifluoroacetylamino)hexyl 2-acetamido-2,6-dideoxy-beta-D-glucopyranoside and 2-acetamido-2-deoxy-alpha-D-xylopyranoside, two allyl 2-acetamido-2-deoxy-alpha-D-glucopyranosiduronic acid derivatives, and several allyl 2-acylamido-2-deoxy-beta-D-glucopyranosides having different acyl groups. These and other compounds were used as inhibitors in the binding assay for the chicken hepatic lectin specific for N-acetylglucosamine. We found that: 1) The inhibitory potency of N-acylglucosamine derivatives decreased progressively with increase in the size of acyl group, 2) absence of either 3- or 4-OH group of N-acetylglucosamine lowered the binding affinity more than 100-fold, and 3) the presence of a negatively charged group (carboxylic acid) at the C-6 position did not lower the affinity. The first two items are similar to the mammalian hepatic galactose/N-acetylgalactosamine lectins, but the last item is in a strong contrast to the mammalian lectins."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":13,"end":32},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T2","span":{"begin":559,"end":578},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T3","span":{"begin":760,"end":779},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T4","span":{"begin":1002,"end":1011},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T5","span":{"begin":1002,"end":1011},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T6","span":{"begin":1012,"end":1033},"obj":"https://glytoucan.org/Structures/Glycans/G27025MB"}],"text":"Synthesis of N-acetylglucosamine derivatives as probes for specificity of chicken hepatic lectin.\nSyntheses of the following compounds are described: 6-(Trifluoroacetylamino)hexyl 2-acetamido-2,6-dideoxy-beta-D-glucopyranoside and 2-acetamido-2-deoxy-alpha-D-xylopyranoside, two allyl 2-acetamido-2-deoxy-alpha-D-glucopyranosiduronic acid derivatives, and several allyl 2-acylamido-2-deoxy-beta-D-glucopyranosides having different acyl groups. These and other compounds were used as inhibitors in the binding assay for the chicken hepatic lectin specific for N-acetylglucosamine. We found that: 1) The inhibitory potency of N-acylglucosamine derivatives decreased progressively with increase in the size of acyl group, 2) absence of either 3- or 4-OH group of N-acetylglucosamine lowered the binding affinity more than 100-fold, and 3) the presence of a negatively charged group (carboxylic acid) at the C-6 position did not lower the affinity. The first two items are similar to the mammalian hepatic galactose/N-acetylgalactosamine lectins, but the last item is in a strong contrast to the mammalian lectins."}