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Article

An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases.

Journal of biochemistry - 1 Jul 1996

Adachi T, Morihara N, Yamazaki N, Yamada H, Futenma A, Kato K, Hirano K

Abstract excerpt

Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandström, J. et al. (1994) J. Biol. Chem. 269, 19163-19166], which causes the impairment of its binding ability to endothelial cell surface...

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PMID: 8864862
DOI: 10.1093/oxfordjournals.jbchem.a021383

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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