Abstract:
:The sodA gene coding for manganese superoxide dismutase (Mn-SOD) from the marine microorganism Vibrio parahaemolyticus was cloned, sequenced, and overexpressed in Escherichia coli by use of the pET20b (+) expression vector. The full-length gene consisted of a 588-bp open reading frame and encoded a polypeptide of 196 amino acid residues, with a calculated molecular mass of 21,713 Da. The recombinant enzyme was efficiently purified from crude E. coli cell lysate by metal ion affinity chromatography. The recombinant VPMn-SOD resisted thermo-denaturation up to 60 degrees C and was insensitive to such inhibitors as EDTA, NaN3 and diethyldithiocarbamic acid. The specificity of V. parahaemolyticus Mn-SOD gene probe was analyzed by cross-species polymerase chain reaction to provide information for Vibrio strain identification.
journal_name
IUBMB Lifejournal_title
IUBMB lifeauthors
Shyu YC,Lin FPdoi
10.1080/713803521keywords:
subject
Has Abstractpub_date
1999-09-01 00:00:00pages
345-52issue
3eissn
1521-6543issn
1521-6551journal_volume
48pub_type
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