Overproduction in Escherichia coli and Purification of the Hemolytic Protein Sticholysin II from the Sea Anemone Stichodactyla helianthus
Copyright policy )Overproduction in Escherichia coli and Purification of the Hemolytic Protein Sticholysin II from the Sea Anemone Stichodactyla helianthus
The cDNA coding for the cytolytic toxins sticholysin I and sticholysin II from the sea anemone Stichodactyla helianthus has been isolated, cloned in pUC18, and sequenced. A 6His-tagged version of sticholysin II has been overproduced in Escherichia coli and purified to homogeneity in milligram amounts. Conformational and functional analyses of recombinant sticholysin II do not reveal any significant difference when compared to the natural cytolysin.
DNA, Complementary, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Hemolysin Proteins, Cnidarian Venoms, Sea Anemones, Escherichia coli, Animals, Amino Acid Sequence, Cloning, Molecular, Organic Chemicals, DNA Primers
DNA, Complementary, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Recombinant Proteins, Hemolysin Proteins, Cnidarian Venoms, Sea Anemones, Escherichia coli, Animals, Amino Acid Sequence, Cloning, Molecular, Organic Chemicals, DNA Primers
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