barbula/superoxide dismutase

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Isolation of a germin-like protein with manganese superoxide dismutase activity from cells of a moss, Barbula unguiculata.

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A novel extracellular Mn-superoxide dismutase (SOD) was isolated from a moss, Barbula unguiculata. The SOD was a glycoprotein; the apparent molecular mass of its native form was 120 kDa, as estimated by gel filtration chromatography, and that of its monomer was 22,072 Da, as estimated by time of

Identification of negative cis-acting elements in response to copper in the chloroplastic iron superoxide dismutase gene of the moss Barbula unguiculata.

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Superoxide dismutases (SODs) are ubiquitous metalloenzymes that catalyze the dismutation of superoxide radicals. Chloroplasts have two isozymes, copper/zinc SOD (Cu/ZnSOD) and iron SOD (FeSOD), encoded by nuclear genes. Because bryophytes are considered as the earliest land plants, they are one of

Germin-like protein gene family of a moss, Physcomitrella patens, phylogenetically falls into two characteristic new clades.

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We identified 77 EST clones encoding germin-like proteins (GLPs) from a moss, Physcomitrella patens in a database search. These Physcomitrella GLPs ( PpGLP s) were separated into seven groups based on DNA sequence homology. Phylogenetic analysis showed that these groups were divided into two novel

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