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J. Biol. Chem., Vol. 275, Issue 47, 36726-36733, November 24, 2000
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From the Department of Biochemistry, Biophysics, and Molecular
Biology, Iowa State University, Ames, Iowa 50011
Nectarin I, a protein that accumulates in the
nectar of Nicotiana sp., was determined to contain
superoxide dismutase activity by colorimetric and in-gel assays. This
activity was found to be remarkably thermostable. Extended incubations
at temperatures up to 90 °C did not diminish the superoxide
dismutase activity of nectarin I. This attribute allowed nectarin I to
be purified to homogeneity by heat denaturation of the other nectar
proteins. By SDS-polyacrylamide gel electrophoresis, nectarin I
appeared as a 29-kDa monomer. If the protein sample was not boiled
prior to loading the gel, then nectarin I migrated as 165-kDa
oligomeric protein. By matrix-assisted laser desorption/ionization
time-of-flight mass spectrometry, the protomer subunit was found to be
a 22.5-kDa protein. Purified nectarin I contained 0.5 atoms of
manganese/monomer, and the superoxide dismutase activity of nectarin I
was not inhibited by either H2O2 or NaCN.
Following denaturation, the superoxide dismutase activity was restored
after Mn2+ addition. Addition of Fe2+,
Cu2+, Zn2+, and
Cu2+/Zn2+ did not restore superoxide dismutase
activity. The quaternary structure of the reconstituted enzyme was
examined, and only tetrameric and pentameric aggregates were
enzymatically active. The reconstituted enzyme was also shown to
generate H2O2. Putative nectarin I homologues were found in the nectars of several other plant species.
Tobacco Nectarin I
PURIFICATION AND CHARACTERIZATION AS A GERMIN-LIKE, MANGANESE
SUPEROXIDE DISMUTASE IMPLICATED IN THE DEFENSE OF FLORAL REPRODUCTIVE
TISSUES*
*
This work was supported by the Carver Trust, the Hatch Act,
and State of Iowa funds. This is Journal Paper J-18949 of the Iowa
Agriculture and Home Economics Experiment Station (Ames, IA), Project
3340.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry
and Biophysics, 2212 Molecular Biology Bldg., Iowa State University,
Ames, IA 50011. Tel.: 515-294-7885; Fax: 515-294-0453; E-mail:
thorn@iastate.edu.
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