High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris

Protein Expression and Purification

Volumn 21, Issue 1, 2001, Pages 210-219

  Hartleib, Judith ^a   Rüterjans, Heinz ^a  

^a GOETHE UNIVERSITY   (Germany)

Author keywords

Bacterial expression; Diisopropylfluorophosphatase; Limited proteolysis; Organophosphates; Refolding screen

Indexed keywords

AMINO ACID SEQUENCE; BACTERIAL GENE; CELL INCLUSION; DIISOPROPYLFLUOROPHOSPHATASE; ENZYME SPECIFICITY; ENZYMIC DEGRADATION; GENE EXPRESSION SYSTEM; ION EXCHANGE CHROMATOGRAPHY; ORGANOPHOSPHATE; PROTEIN DOMAIN; PROTEINASE;

ESCHERICHIA COLI; LOLIGO VULGARIS;

EID: 0034958633     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1360     Document Type: Article

References (36)

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17. Comparison of DFP-hydrolyzing enzyme purified from head ganglion and hepatopancreas of squid (Loligo pealei) by means of isoelectric focusing
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19. A partial primary structure of squid hepatopancreas organophosphorus acid hydrolase
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21. Measurement of protein by spectrophotometry at 205 nm
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27. Proteolytic mapping of heat shock transcription factor domains
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29. Domain structure and intramolecular regulation of dynamin GTPase
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31. Use of the T7 RNA polymerase to direct expression of cloned genes
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