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It is the only <jats:styled-content style=\"fixed-case\">SOD<\/jats:styled-content> isozyme that is secreted and glycosylated (at asparagine 89). However, the physiological roles of its glycosylation are poorly understood. In this study, we found that the glycosylation site on <jats:styled-content style=\"fixed-case\">EC<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">SOD<\/jats:styled-content> is well conserved and that a glycosylation\u2010deficient <jats:styled-content style=\"fixed-case\">EC<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">SOD<\/jats:styled-content> mutant retains its enzymatic activity, but is not secreted. This impairment in secretion may, in part, be due to the ability of the mutants to form unusual higher order oligomers. 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