Abstract:
Disclosed are compositions and methods for decreasing the viscosity and/or cohesiveness of and/or increasing the liquefaction of excessively or abnormally viscous or cohesive mucus or sputum. The composition contains a protein or peptide containing a thioredoxin monocysteinic active site in a reduced state and optionally further contains a reducing system.
Abstract:
Provided herein are methods for expressing proteins with disulfide bridges such as Vicrostatin (VCN), a chimeric variant of native snake venom disintegrin Contortrostatin (CN). The methods include what is believed to be a more efficient natural selection process that results in generating increased amounts of correctly-folded active conformers of proteins with disulfide bridges. In an aspect, this is achieved by growing Origami B cells in a more optimal redox environment during the induction of heterologous recombinant protein production.
Abstract:
Disclosed are compositions and methods for decreasing the viscosity and/or cohesiveness of and/or increasing the liquefaction of excessively or abnormally viscous or cohesive mucus or sputum. The composition contains a protein or peptide containing a thioredoxin active-site in reduced state and optionally further contains a reducing system.
Abstract:
Thioredoxin, a small dithiol protein, is a specific reductant for allergenic proteins and particularly allergenic proteins present in pollen and animal and plant sources. All targeted proteins contain disulfide (S—S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active and less digestible in the oxidized (S—S) state. When reduced (SH state), they lose their allergenicity and/or become more digestible. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by lipoic acid chemical reductant. Skin tests carried out with sensitized dogs showed that treatment of the pollens with reduced thioredoxin prior to injection eliminated or decreased the allergenicity of the pollen. Studies showed increased digestion of the pollen proteins by pepsin following reduction by thioredoxin. Pollen proteins that have been reduced by thioredoxin are effective and safe immunotherapeutic agents for decreasing or eliminating an animal's allergic reaction that would otherwise occur upon exposure to the non-reduced pollen protein.
Abstract:
The present invention relates to the use of a variety of methods for generating functional thioredoxin reductase variants in which at least one physical, chemical or biological property of the variant is altered in a specific and desired manner when compared to the wild-type protein.
Abstract:
The present invention relates to the use of a variety of methods for generating functional thioredoxin reductase variants in which at least one physical, chemical or biological property of the variant is altered in a specific and desired manner when compared to the wild-type protein.
Abstract:
An AhpF protein has thioredoxin reductase, peroxidase, and chaperone activities and is derived from Pseudomonas aeruginosa, and a use therefor. By using a novel activity of the AhpF of Pseudomonas aeruginosa according to the present invention, it is possible to produce a plant having strong resistance to various environmental stresses such as oxidative stress or heat stress, thereby making it possible to contribute to increasing crop productivity and mass production of useful constituents. In addition, it is possible to prevent desertification and environmental pollution through the development of transformed plants having resistance to high temperatures and drying.
Abstract:
Provided is a process for the preparation of L-methionine in an enzymatic reaction utilizing dimethyl disulfide (DMDS) a precursor of L-methionine, and an organic reducing compound. In the process, methyl mercaptan can be formed by the enzymatic hydrogenolysis of the DMDS.
Abstract:
Disclosed are compositions and methods for decreasing the viscosity and/or cohesiveness of and/or increasing the liquefaction of excessively or abnormally viscous or cohesive mucus or sputum. The composition contains a protein or peptide containing a thioredoxin active-site in reduced state and optionally further contains a reducing system.
Abstract:
Provided herein are methods for expressing proteins with disulfide bridges such as Vicrostatin (VCN), a chimeric variant of native snake venom disintegrin Contortrostatin (CN). The methods include what is believed to be a more efficient natural selection process that results in generating increased amounts of correctly-folded active conformers of proteins with disulfide bridges. In an aspect, this is achieved by growing Origami B cells in a more optimal redox environment during the induction of heterologous recombinant protein production.