Fast purification of thioredoxin reductases and of thioredoxins with an unusual redox-active centre from anaerobic, amino-acid-utilizing bacteria

Article Abstract:

The thioredoxin system consists of the two proteins NADPH-dependent thioredoxin reductase and thioredoxin, both of which are redox-active, with two cysteine residues. They are mainly involved in catabolic metabolism. A method for the purification of thioredoxin reductase and thioredoxin from Eubacterium acidaminophilum, Clostridium litorale, C. sporogenes, C. Cylindrosporum and C. Sticklandii, was developed. None of the thioredoxins reacted with thioredoxin reductase of E. coli, although there was interaction with the thioredoxin reductases from other anaerobes.

Observations, Metabolism, Anaerobic bacteria

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Expression of disulphide-bridge-dependent conformational epitopes and immunogenicity of the carboxy-terminal 19 kDa domain of plasmodium yoelii merozoite surface protein-1 in live attenuated Salmonella vaccine strains

Article Abstract:

A study was conducted to analyze the expression of the 19 kDa carboxy-terminal domain of Plasmodium yoelii merozoite surface protein in Salmonella vaccine strains as a carboxy-terminal fusion to fragment C of tetanus toxin. The design of live multivalent bacterial vaccines against eukaryotic pathogens was also examined. Experimental results indicated that the lack of protection correlated with the antibody response.

Research, Proteins, Pathogenic microorganisms, Tetanus, Antibodies

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