Abstract: The invention describes compositions and methods of use for 2,5-dihydroxybenzene sulfonic acid compounds and pharmaceutically acceptable salts thereof. The invention provides methods for (a) treating skin cancer; (b) treating cancer of the organs; (c) treating leukemia; (d) improving the efficacy of chemotherapy, radiation therapy and/or cancer immunotherapy; (e) treating rosacea; and (f) treating psoriasis by administration of a composition comprising at least one 2,5-dihydroxybenzene sulfonic acid compound or a pharmaceutically acceptable salt thereof, and, optionally at least one therapeutic agent. Also disclosed are compositions comprising administration of at least one 2,5-dihydroxybenzene sulfonic acid compound, or a pharmaceutically acceptable salt thereof, and, at least one therapeutic agent.

Abstract: A naphthalenesulfonic acid or quinolinesulfonic acid of formula (I), wherein A is N or a CR8 formula group, where R8 is H, OH, NR10R11, independently from one another, where R10 and R11 represent H or C1-C6 alkyl or a group of formula NH—CO—R12, where R12 is C1-C6 alkyl or C6-C10 aryl; R1 and R2 represent H or SO3R9, independently from one another, where R9 is H, ammonium or a cation of an alkali or alkaline-earth metal; R3 is H or OH; and R4, R5, R6 and R7 represent H, an NR10R11 or NH—CO—R12 group, independently from one another; on the condition that (i) at least one of R1 or R2 is SO3R9, and (ii) at least one of R4, R5, R6 or R7 is an NR10R11 or NH—CO—R12 group, or their pharmaceutically acceptable salts; and a pharmaceutically acceptable excipient.

Abstract: Methods of reducing cystine containing animal and plant proteins, and improving dough and baked goods' characteristics is provided which includes the steps of mixing dough ingredients with a thiol redox protein to form a dough and baking the dough to form a baked good. The method of the present invention preferably uses reduced thioredoxin with wheat flour which imparts a stronger dough and higher loaf volumes. Methods for reducing snake, bee and scorpion toxin proteins with a thiol redox (SH) agent and thereby inactivating the protein or detoxifying the protein in an individual are also provided. Protease inhibitors, including the, Kunitz and Bowman-Birk trypsin inhibitors of soybean, were also reduced by the NADP/thioredoxin system (NADPH, thioredoxin, and NADP-thioredoxin reductase) from either E. coli or wheat germ. When reduced by thioredoxin, the Kunitz and Bowman-Birk soybean trypsin inhibitors lose their ability to inhibit trypsin.

Abstract: Thioredoxin, a small dithiol protein, is a specific reductant for major allergenic proteins present in widely used foods from animal and plant sources. All targeted allergenic proteins contain disulfide (S—S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active in the oxidized (S—S) state. When reduced (SH state), they lose their allergenicity. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by dithiothreitol, a chemical reductant. Skin tests and feeding experiments carried out with sensitized dogs showed that treatment of the food with reduced thioredoxin prior to ingestion eliminated or decreased the allergenicity of the food.

Abstract: Methods of reducing cystine containing animal and plant proteins, and improving dough and baked goods' characteristics is provided which includes the steps of mixing dough ingredients with a thiol redox protein to form a dough and baking the dough to form a baked good. The method of the present invention preferably uses reduced thioredoxin with wheat flour which imparts a stronger dough and higher loaf volumes. Methods for reducing snake, bee and scorpion toxin proteins with a thiol redox (SH) agent and thereby inactivating the protein or detoxifying the protein in an individual are also provided. Protease inhibitors, including the Kunitz and Bowman-Birk trypsin inhibitors of soybean, were also reduced by the NADP/thioredoxin system (NADPH, thioredoxin, and NADP-thioredoxin reductase). When reduced by thioredoxin, the Kunitz and Bowman-Birk soybean trypsin inhibitors lose their ability to inhibit trypsin.

Abstract: Methods of reducing cystine containing animal and plant proteins, and improving dough and baked goods' characteristics is provided which includes the steps of mixing dough ingredients with a thiol redox protein to form a dough and baking the dough to form a baked good. The method of the present invention preferably uses reduced thioredoxin with wheat flour which imparts a stronger dough and higher loaf volumes. Methods for reducing snake, bee and scorpion toxin proteins with a thiol redox (SH) agent and thereby inactivating the protein or detoxifying the protein in an individual are also provided. Protease inhibitors, including the Kunitz and Bowman-Birk trypsin inhibitors of soybean, were also reduced by the NADP/thioredoxin system (NADPH, thioredoxin, and NADP-thioredoxin reductase) from either E. coli or wheat germ. When reduced by thioredoxin, the Kunitz and Bowman-Birk soybean trypsin inhibitors lose their ability to inhibit trypsin.

Abstract: A method is used for monitoring network traffic. For a plurality of time periods, percent utilization of one or more network segments is determined. This is done in order to generate utilization data. The utilization data is organized to produce organized utilization data. The first organized utilization data indicates a percent frequency of the plurality of time periods during which the first network segment is at least equal to each value of percent utilization. The first organized utilization data is displayed in a graph. The graph has a first axis which indicates percent utilization and a second axis which indicates percent frequency.

Abstract: Thioredoxin, a small dithiol protein, is a specific reductant for major allergenic proteins present in widely used foods from animal and plant sources. All targeted allergenic proteins contain disulfide (S--S) bonds that are reduced to the sulfhydryl (SH) level by thioredoxin. The proteins are allergenically active in the oxidized (S--S) state. When reduced (SH state), they lose their allergenicity. Thioredoxin achieved this reduction when activated (reduced) either by NADPH via NADP-thioredoxin reductase (physiological conditions) or by dithiothreitol, a chemical reductant. Skin tests and feeding experiments carried out with sensitized dogs showed that treatment of the food with reduced thioredoxin prior to ingestion eliminated or decreased the allergenicity of the food.