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J Biol Chem, Vol. 274, Issue 47, 33274-33278, November 19, 1999
,
From the Department of Biological Science, Faculty of Science,
Hiroshima University, Kagamiyama,
Higashi-Hiroshima 739-8526, Japan, the 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 flight mass
spectroscopy. The protein had manganese with a stoichiometry of 0.80 Mn/monomer. The cDNA clone for a gene encoding the extracellular
Mn-SOD was isolated. Sequence analysis showed that it has a strong
similarity to germin (oxalate oxidase) and germin-like proteins (GLPs)
of several plant species and possesses all the characteristic features of members of the germin family. The clone encoding this extracellular Mn-SOD was therefore designated B. unguiculata GLP
(BuGLP). BuGLP had no oxalate oxidase activity. In
addition, the cDNA for a gene encoding the moss mitochondrial
Mn-SOD was isolated. Its amino acid sequence had little similarity to
that of BuGLP, even though a close similarity was observed among the
mitochondrial Mn-SODs of various organisms. BuGLP was the first
germin-like protein that was really demonstrated to be a metalloprotein
with Mn-SOD activity but no oxalate oxidase activity.
Department of
Biological Science, Faculty of Science, Kumamoto University, Kurokami,
Kumamoto 860-8555, Japan, and the § Department of Applied
Biological Chemistry, The University of Tokyo, Bunkyou-ku,
Tokyo 113-8657, Japan
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