Format

Send to

Choose Destination
Biosci Biotechnol Biochem. 2007 Apr;71(4):1090-3. Epub 2007 Apr 7.

Purification, characterization, and molecular cloning of a thermostable superoxide dismutase from Thermoascus aurantiacus.

Author information

1
Department of Environmental Biology, Shandong Agricultural University, Taian, Shandong, China.

Abstract

A thermostable superoxide dismutase [(SOD) EC 1.15.1.1] from a Thermoascus aurantiacus var. levisporus was purified to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) homogeneity by a series of column chromatographies. The molecular mass of a single band of the enzyme was estimated to be 16.8 kDa by SDS-PAGE. The molecular mass was estimated to be 33.2 kDa by gel filtration on Sephacryl S-100, indicating that the enzyme was composed of two identical subunits of 16.8 kDa each. N-terminal amino acid sequencing (seven residues) yielded VKAVAVL. Using RACE-PCR, a Cu, Zn-SOD gene was cloned from T. aurantiacus var. levisporus. The sequence was 705 bp and contained a 468 bp ORF encoding a Cu, Zn-SOD of 155 amino acid residues.

PMID:
17420576
DOI:
10.1271/bbb.60709
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
Loading ...
Support Center