Abstract: The expression vectors and methods using an E. coli expression system for the large scale production of FGF18 are described. The vectors utilize the FGF18 coding sequence with specific changes in nucleotides in order to optimize codons and mRNA secondary structure for translation in E. coli. Using the expression vectors, the FGF18 gene was produced in E. coli to a level of greater than 1 g/L in fed batch fermentation. Also included are OmpT deficient E. coli strains, as well as OmpT and fhuA negative strains transformed with an FGF18 expression vector.

Abstract: The invention is directed to methods for purifying Troponin I, particularly recombinant Tropnin I produced in a bacterial expression system. Recombinant Tropnin I can be advantageously purified after reversibly protecting the free sulfhydryl groups, e.g., by forming sulfates. In a specific example, Tropnin I reacted with sodium tetrafhionate yielded sulfitolyzed Tropnin I, which was purified by chromatography on an anion exchanger, followed by hydrophobic interaction chromatography. Facile deprotection of the sulfhydryl groups yields a highly purified product ready for refolding.

Abstract: The invention is directed to methods for purifying Troponin I, particularly recombinant Troponin I produced in a bacterial expression system. Recombinant Troponin I can be advantageously purified after reversibly protecting the free sulfhydryl groups, e.g., by forming sulfates. In a specific example, Tropnin I reacted with sodium tetrafhionate yields sulfitolyzed Tropnin I, which was purified by chromatography on an anion exchanger, followed by hydrophobic interaction chromatography. Facile deprotection of the sulfhydryl groups yields a highly purified product ready for refolding.

Abstract: The invention is directed to methods for purifying Troponin I, particularly recombinant Tropnin I produced in a bacterial expression system. Recombinant Tropnin I can be advantageously purified after reversibly protecting the free sulfhydryl groups, e.g., by forming sulfates. In a specific example, Tropnin I reacted with sodium tetrafhionate yielded sulfitolyzed Tropnin I, which was purified by chromatography on an anion exchanger, followed by hydrophobic interaction chromatography. Facile deprotection of the sulfhydryl groups yields a highly purified product ready for refolding.

Abstract: The invention is directed to methods for purifying Troponin I, particularly recombinant Tropnin I produced in a bacterial expression system. Recombinant Tropnin I can be advantageously purified after reversibly protecting the free sulfhydryl groups, e.g., by forming sulfates. In a specific example, Tropnin I reacted with sodium tetrafhionate yielded sulfitolyzed Tropnin I, which was purified by chromatography on an anion exchanger, followed by hydrophobic interaction chromatography. Facile deprotection of the sulfhydryl groups yields a highly purified product ready for refolding.

Abstract: The invention is directed to methods for purifying Troponin I, particularly recombinant Tropnin I produced in a bacterial expression system. Recombinant Tropnin I can be advantageously purified after reversibly protecting the free sulfhydryl groups, e.g., by forming sulfates. In a specific example, Tropnin I reacted with sodium tetrafhionate yielded sulfitolyzed Tropnin I, which was purified by chromatography on an anion exchanger, followed by hydrophobic interaction chromatography. Facile deprotection of the sulfhydryl groups yields a highly purified product ready for refolding.