Abstract: A monopropellant thruster according to an exemplary aspect of the present disclosure includes, among other things, a first part having a catalyst bed, a thrust chamber, and a nozzle. The first part is integrally formed via a single additive manufacturing process. The thruster further includes a second part, which is a closeout. A method is also disclosed.

Abstract: It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T-cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by altering as little as a single amino acid within the protein, preferably a hydrophobic residue towards the center of the IgE epitope, to eliminate IgE binding. Additionally or alternatively a modified allergen with reduced IgE binding may be prepared by disrupting one or more of the disulfide bonds that are present in the natural allergen. The disulfide bonds may be disrupted chemically, e.g., by reduction and alkylation or by mutating one or more cysteine residues present in the primary amino acid sequence of the natural allergen. In certain embodiments, modified allergens are prepared by both altering one or more linear IgE epitopes and disrupting one or more disulfide bonds of the natural allergen.

Abstract: It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE-binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than-within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined.

Abstract: The invention provides a device for the detection and mapping of radiation, the device comprising a polymeric core located within an external shell material, wherein the polymeric core comprises at least one radiation sensitive component and the external sheath comprises a collimation sheath. Preferably, the polymeric core comprises a spherical core which is encased within the external shell. The external shell is preferably comprised of a metal, most preferably lead or tungsten.

Abstract: It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity. The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined.

Abstract: It is desirable to be able to securely connect individual electrical components within an electrical module. An electrical module is provided in which a plurality of energy storage components are connected together using a clamp instead of wiring or bus bar connections. In one configuration, for example, a first energy storage component comprising a first terminal and second terminal is connected to a second energy storage component comprising a third terminal and a fourth terminal. The first terminal of the first energy storage component is electrically connected to a third terminal of the second energy storage component using a clamp comprising a recess. The recess of the clamp receives at least a portion of the first terminal of the first energy storage component and at least a portion of the third terminal of the second energy storage component.

Abstract: One of the major peanut allergens, Ara h I, was selected from cDNA expression library clones using Ara h I specific oligo-nucleotides and polymerase chain reaction technology. The Ara h I clone identified a 2.3 kb mRNA species on a Northern blot containing peanut poly A+RNA. DNA sequence analysis of the cloned inserts revealed that the Ara h I allergen has significant homology with the vicilin seed storage protein family found in most higher plants. The isolation of the Ara h I clones allowed the synthesis of this protein in E. coli cells and subsequent recognition of this. recombinant protein in immunoblot analysis using serum IgE from patients with peanut hypersensitivity.

Abstract: It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T-cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by altering as little as a single amino acid within the protein, preferably a hydrophobic residue towards the center of the IgE epitope, to eliminate IgE binding. Additionally or alternatively a modified allergen with reduced IgE binding may be prepared by disrupting one or more of the disulfide bonds that are present in the natural allergen. The disulfide bonds may be disrupted chemically, e.g., by reduction and alkylation or by mutating one or more cysteine residues present in the primary amino acid sequence of the natural allergen. In certain embodiments, modified allergens are prepared by both altering one or more linear IgE eitopes and disrupting one or more disulfide bonds of the natural allergen.

Abstract: Peanuts are a common cause of food hypersensitivity reactions. The sera of 10 patients who had atopic dermatitis and a positive double-blind placebo-controlled food challenge to peanut were used to investigate the major allergens of peanut. Crude Florunner extracts were fractionated by anion-exchange chromatography using a step gradient (limit buffer, 0.05M BisTris/1.5M NaCl). A protein peak (OD 280) which eluted at 10% NaCl and demonstrated intense IgE-binding was further analyzed by two-dimensional SDS-PAGE/immunoblot analysis. The majority of this fraction is a protein which has a molecular weight of 17 kD and a pI of 5.2. Sequencing data from the N-terminus revealed the following initial 9 amino acids: (*)-Q-Q-(*)-E-L-Q-D-L. Based on IgE-binding activity and no known amino acid sequence identity to other allergens, this allergen is designated Ara h II. Ara h II may be used to detect and quantify peanut allergens in foodstuffs.

Abstract: A frozen nutritional food product and method for oral delivery of nutrients, medicinal substances and other active ingredients via absorption through the oral mucosa for systemic effect. The frozen product includes at least one active ingredient, at least one flavoring agent, preservatives, food coloring, and a balance of water as a delivery liquid. The water is subjected to a magnetic treatment process and an ozonation process to enhance delivery of the active ingredients. More particularly, a first portion of the water is magnetized to neutralize the pH, increase oxygenation, and to improve the solubility of the ingredients mixed with the water. The remaining portion of the water is sterilized by ozonation, causing oxidation of undesirable metallic ions, odor and taste producing agents, and a wide variety of organics. Ozonation further increases the dissolved oxygen content of the water.

Abstract: The invention encompasses a frozen composition containing an active ingredient. The active ingredients include but are not limited to a nutrient mixture and a medicine. In its preferred embodiment, the chemical composition contains the following ingredients: a nutrient mixture, at least one flavoring agent, preservatives, food coloring, and a balance of water. The composition can be placed in a sealed plastic bag and frozen to form a nutrient enriched ice pop. Alternatively, the composition can be frozen in-situ, either with or without a stick inserted therein. The invention also includes methods of consuming the composition.