Non-caloric artificial sweeteners (NAS) are used as a substitute for natural sugars by providing the sweet taste. This invention measures the effects of artificial sweeteners on the enzyme kinetics of biological systems. The claimed invention is directed to a method of measuring the effect of an artificial sweetener on enzyme-catalyzed hydrolysis of a sugar comprising establishing a first sugar enzymatic conversion rate, then determining a second sugar enzymatic conversion rate, and lastly comparing the first sugar enzymatic rate and the second sugar enzymatic conversion rate. The sugar enzymatic conversion rates can be measured by either nuclear magnetic resonance spectroscopy or a glucometer. The methodology presented may be applied to the elucidation of kinetic parameters for invertase catalyzed conversion of sucrose to glucose and fructose.

Apparatus and methods for the detection of proteins in biological fluids such as urine using a label-free assay is described. Specific proteins are detected by their binding to highly specific capture reagents such as SOMAmers that are attached to the surface of a substrate. Changes to these capture reagents and their local environment upon protein binding modify the behavior of color centers (e.g., fluorescence, ionization state, spin state, etc.) embedded in the substrate beneath the bound capture reagents. These changes can be read out, for example, optically or electrically, for an individual color center or as an average response of many color centers.

A method for the qualification and selection of manufacturing processes, raw materials, intermediates and batch production of pentosan polysulfate based on the identification of acetylated monosaccharide units, including units of xylose substituted with 4-O-methyl-glucuronic which also lead the acetyl group, as structural characterizing units, is disclosed.

A magnetic resonance device for monitoring growth of tissue in one or more bioreactors. The device can include a first magnet and a second magnet that can form a uniform magnetic field of desired strength around at least one sample of effluent from at least one bioreactor. At the command of a controller, an RF signal can illuminate the at least one magnetized sample, and sensors can detect at least one echo signal from the at least one magnetized sample. The controller can characterize the at least one sample based on the at least one echo signal. A resonator can shape the at least one echo signal.

Computing systems and methods for characterizing a protein are provided. Each residue in a subset of the protein is in an amino acid type set and is represented by a vertex in a graph G formed from an atomic model of the protein. NMR data, acquired with some of the residues of the protein isotopically labeled, is used to form a graph H with each vertex representing a different residue of the protein and assigned one or more amino types. Placements of H onto G are formed, each including mappings assigning vertices in H to vertices in G subject to the constraints that vertices in H mapped to vertices in G cannot be of different amino acid types and edges between pairs of vertices in H must map to corresponding edges in G. For each vertex in H, the number of different valid mappings to G is determined by polling the placements as a constraint satisfaction problem and is deemed assigned when only a single unique assignment is identified.

In a first step, a sample liquid is fabricated by mixing a sample formed of a polyester or decomposition products of a polyester into a solvent. The solvent used here contains chloroform and 2,2,2-trifluoroethanol and has an organic base added thereto. The organic base is at least one of a primary amine, a secondary amine, a tertiary amine and a heterocyclic amine. Next, in a second step, each of the amount of the terephthalic acid terminal and the amount of the hydroxy group terminal in the sample liquid is measured through a nuclear magnetic resonance spectroscopy aiming at hydrogen atoms. Subsequently, in a third step, the number average molecular weight of the sample is calculated from the amount of the terephthalic acid terminal and the amount of the hydroxy group terminal measured in the second step.

This invention relates to a method of determining ligands of macromolecules, said method comprising or consisting of (a) subjecting a sample comprising (i) complexes formed by said macromolecules and said ligands and (ii) unbound ligands to a method which separates said complexes from said unbound ligands; (b) releasing ligands from complexes obtained in step (a); and (c) subjecting the released ligands obtained in step (b) to a chemical analysis method, thereby determining said ligands of said macromolecules.

Apparatus and methods for the detection of proteins in biological fluids such as urine using a label-free assay is described. Specific proteins are detected by their binding to highly specific capture reagents such as SOMAmers that are attached to the surface of a substrate. Changes to these capture reagents and their local environment upon protein binding modify the behavior of color centers (e.g., fluorescence, ionization state, spin state, etc.) embedded in the substrate beneath the bound capture reagents. These changes can be read out, for example, optically or electrically, for an individual color center or as an average response of many color centers.

A chemical bond evaluation method capable of directly evaluating the presence or absence of a chemical bond between silica and a silane coupling agent includes performing multidimensional solid-state nuclear magnetic resonance (NMR) analysis on a rubber composition comprising a rubber component, a silica, and a silane coupling agent; and evaluating the presence or absence of a chemical bond between silica and the silane coupling agent in the rubber composition containing a rubber component, the silica, and the silane coupling agent.

A defined peak region residing between about 3.2 and 3.4 ppm of a proton NMR spectrum of an in vitro biosample is electronically evaluated to determine a level of trimethylamine-N-oxide (TMAO). The biosample may be any suitable biosamples including human serum with a normal biologic range of between about 1-50 ?M or urine with a normal biologic range of between about 0-1000 ?M.