| http://purl.uniprot.org/citations/1505778 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1505778 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1505778 | http://www.w3.org/2000/01/rdf-schema#comment | "The secretory enzyme extracellular-superoxide dismutase (EC-SOD) has affinity for heparin and some other sulfated glycosaminoglycans and is in vivo bound to heparan sulfate proteoglycan. Nonenzymic glycation of EC-SOD, both in vivo and in vitro, is associated with a reduction in heparin affinity, whereas the enzymic activity is not affected. The glycation sites in EC-SOD are further studied in the present article. It is shown that modification of a few of the five lysyl residues of the subunits of the enzyme with trinitrobenzene sulfonic acid nearly abolishes the in vitro glycation susceptibility. From a chymotryptic digest of in vitro glycated EC-SOD, two peptides with affinity for boronate could be isolated. Amino acid sequence analysis showed that both encompassed the carboxyterminal end. epsilon-Glucitol lysine was identified in both peptides at positions 211 and 212. The primary glycation sites in EC-SOD are thus lysine-211 and lysine-212 in the putative heparin-binding domain in the carboxyterminal end."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.org/dc/terms/identifier | "doi:10.1016/0891-5849(92)90016-a"xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.org/dc/terms/identifier | "doi:10.1016/0891-5849(92)90016-a"xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Adachi T."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Adachi T."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Hayashi K."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Hayashi K."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Ohta H."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Ohta H."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Hirano K."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Hirano K."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Marklund S.L."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/author | "Marklund S.L."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/name | "Free Radic. Biol. Med."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/name | "Free Radic. Biol. Med."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/pages | "205-210"xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/pages | "205-210"xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/title | "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/title | "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro."xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/1505778 | http://purl.uniprot.org/core/volume | "13"xsd:string |