PubMed:3779697 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":124},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":125,"end":286},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":287,"end":395},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":396,"end":582},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":583,"end":804},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":124},"obj":"Sentence"},{"id":"T2","span":{"begin":125,"end":286},"obj":"Sentence"},{"id":"T3","span":{"begin":287,"end":395},"obj":"Sentence"},{"id":"T4","span":{"begin":396,"end":582},"obj":"Sentence"},{"id":"T5","span":{"begin":583,"end":804},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Non-enzymic glycation of proteins: analysis of N-(1-deoxyhexitol-1-yl)amino acids by high-performance liquid chromatography.\nA method for determining the extent of non-enzymic glycation (originally called \"glycosylation\") of both lysyl and N-terminal residues of a protein is described. The glycated protein is treated with sodium borohydride, and is then subjected to acid-catalysed hydrolysis. The resulting N-(1-deoxy-D-hexitol-1-yl)amino acids are separated by cation-exchange high-performance liquid chromatography (l.c.), and detected by a post-column reaction with periodate. The method has been applied successfully to samples of human hemoglobin and human serum albumin, for measurement of numbers of valine-attached and of lysine-attached N-(1-deoxy-D-fructos-1-yl) groups per protein molecule."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":638,"end":643},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":659,"end":664},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Non-enzymic glycation of proteins: analysis of N-(1-deoxyhexitol-1-yl)amino acids by high-performance liquid chromatography.\nA method for determining the extent of non-enzymic glycation (originally called \"glycosylation\") of both lysyl and N-terminal residues of a protein is described. The glycated protein is treated with sodium borohydride, and is then subjected to acid-catalysed hydrolysis. The resulting N-(1-deoxy-D-hexitol-1-yl)amino acids are separated by cation-exchange high-performance liquid chromatography (l.c.), and detected by a post-column reaction with periodate. The method has been applied successfully to samples of human hemoglobin and human serum albumin, for measurement of numbers of valine-attached and of lysine-attached N-(1-deoxy-D-fructos-1-yl) groups per protein molecule."}