Abstract: Methods of identifying subjects having, or at risk of developing, diabetes, obesity, and/or hypertension are disclosed, as well as methods of identifying biomarkers for diabetes, obesity, and/or hypertension, and biomarkers identified by such methods.

Abstract: A method or platform for monoclonal antibody based biomarker discovery is disclosed. The method according to the invention provides for the integration of analyte collection, hybridoma screening and nanovolume integrated mass spectrometry (NVIMS) to achieve a robust screening system that is capable, for example, of cutting 4-6 years off of the classical biomarker discovery and development process. The invention provides a platform for the rapid, high-throughput production, isolation and characterization of, e.g., disease specific biomarkers together with highly specific monoclonal antibodies. The method of the invention has a variety of applications such as, but not limited to, drug testing, biohazard applications, ecological applications, physiological applications and/or pathology screening applications. The method of the invention is also capable of being performed or used as or with a high-throughput screening process or system of the invention.

Abstract: Methods of identifying subjects having, or at risk of developing, diabetes, obesity, and/or hypertension are disclosed, as well as methods of identifying biomarkers for diabetes, obesity, and/or hypertension, and biomarkers identified by such methods.

Abstract: The invention relates to methods for detecting and identifying potential biomarkers of high-grade cervical dysplasia in an individual human subject. The invention also relates to newly discovered biomarkers, as set forth in Tables 1-4 herein, which are associated with the dysplastic state of cervical cells. It has been discovered that a differential level of expression of any of these markers or combination of these markers correlates with a dysplastic condition in a human subject, e.g., a patient.

Abstract: Methods and systems for providing a user with personalized wellness and health information are described. More particularly, methods and systems are provided for creating an individual health profile display, presented on a network-based interface, based on the analysis of a user-submitted biological sample that has been compared to a knowledge database, and including information related to the comparison.

Abstract: Methods, compositions, and kits related to the use of multi-ligand affinity chromatography are described. The methods include those related to identification of glycoprotein panels for analyzing and diagnosing disease.

Abstract: Described herein are methods and techniques to study the “degradome”. The degradome of a specific protease is the complete product of the natural substrate repertoire of that enzyme in a cell, tissue or organism. The complete set of proteases that are expressed at a particular moment or circumstance by a cell, tissue or organism produces the collective degradome. Included in the methods described herein are approaches that allow the direct identification and characterization of degradome peptides from approx. 400 to approx. 12,000 Da. The methods of the invention avoid the inherent problems of studying the peptidome by focusing on specific or unique proteolytic cleavages that occur as a result of endogenous protease activity induced by specific diseases. Once characterized, the presence of, or change in level of, specific peptides of the degradome can be used, e.g.

Abstract: A combination of “bottom up” and “top down” MS analysis of posttranslational modifications in complex proteins is described. The method comprises digestion of the protein with an enzyme that forms larger peptide fragments than trypsin (>3000 D), performing HPLC with the fragments and applying a new data acquisition strategy using on-line coupling with e.g. LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell. The method is applied to analysis of posttranslational modifications of protein isoforms.

Abstract: An electrophoretic technique is provided for moving a plurality of chemicals into distinct zones for immobilization on a solid surface. The technique includes introducing a first electrolyte and a second electrolyte into a channel, and interposing between the first and second electrolytes at least one solution containing a plurality of chemicals. Under a given electric field, the first electrolyte has anions with higher effective mobility than the chemicals and the second electrolyte has anions with lower effective mobility than the chemicals. When an electrical potential is applied across the length of the channel the plurality of chemicals in the solution are moved into spatial zones. The chemicals in the zones can then be bound to the interior surface of the channel. Chemicals so bound to the wall surface can be used to build very small structures such as arrays and electrical conducting structures.

Abstract: An integrated nucleic acid sample analysis system for matrix-assisted laser-desorption/ionization time-of-flight mass spectroscopy (MALDI-TOF MS) is described. The integrated system comprises a miniaturized sample preparation compartment interfaced directly with a MALDI-TOF ionization surface for amplifying and/or otherwise chemically manipulating an oligonucleotide analyte and presenting the analyte to a MALDI ionization surface for mass spectrometry analysis. The miniaturized integrated sample handling system disclosed herein finds application in the amplification and analysis of DNA samples for genetic diagnosis and other uses.

Abstract: An integrated liquid sample handling system for matrix-assisted laser-desorption/ionization time-of-flight mass spectroscopy (MALDI-TF MS) is described. The integrated system comprises a miniaturized sample handling compartment containing a MALDI ionization surface for separating, chemically manipulating and detecting analytes by MALDI -TOF MS. The miniaturized integrated sample handling system disclosed herein is applicable to a wide range of analytical problems that require separation and/or chemical manipulation of a sample prior to mass analysis as part of the analytical procedure.

Abstract: The present document discloses the formation of imine adducts, preferably between a primary amine of a biologically active polypeptide and a reactive aldehyde group of a physiologically acceptable carrier. The imine adduct of human growth hormone and dextran is specifically described. These adducts serve to release the biologically active polypeptide via the reversible reaction in the formation of the imine adduct bond. These adducts have a surprising degree of stability that permits the use of the complex as a sustained release preparation. A key advantage of this technology is that after hydrolysis the complex releases the unmodified pharmaceutical. Thus, these adducts can be used as pharmaceutical compositions useful for the sustained release of the biologically active polypeptide over a predetermined, desired period of time.

Abstract: Container systems for stable storage of pharmaceutical compounds are disclosed. The container systems prevent the formation of adducts between pharmaceutical compounds and aldehydes during storage of these compounds in containers sealed with elastomeric stoppers that leach aldehydes. Methods for determining the presence of these adducts are also disclosed.

Abstract: There is described a mobile phase for use in the purification of proteins using reversed phase HPLC on a preparative scale. The mobile phase is an aqueous solution containing 0.005 to 1M of a physiologicially acceptable acid of the general formula YCOOH where Y is a polar electron withdrawing group capable of hydrogen bonding silanol groups. The solution also contains up to 95% by volume of a physilogically acceptable organic solvent. A preparative method of purifying proteins such as HSA or BSA and recombinant deoxyribonucleic proteins using reversed phased PHLC is also described.

Abstract: A process is described for removing low density and very low density lipoproteins from blood plasma or serum and recovering the plasma or serum in a physiologically acceptable form. The method involves in a preferred embodiment passing plasma or serum through a cationic ion exchanger equilibrated with a physiologically acceptable saline solution. The ion exchanger is a water insoluble hydrophilic, water swellable cross-linked regenerated or microgranular cellulose matrix substituted with hydroxy C.sub.2 -C.sub.4 alkyl group. The ion exchanger capacity is provided by sulphate groups substituted with from 2 to 6 meq/g. The take up of low density lipoproteins is enhanced by recycling the plasma through the column.

Abstract: The invention relates to the carbonylation of cross linked substituted and unsubstituted polysaccharides, their copolymers with macroporous synthetic polymers, macroporous synthetic polymers and rigid supports with pendant hydroxyalkyl groups. The carbonylated product can be used to prepare an affinity chromatography matrix which remains an uncharged species at varying pH's. The carbonylated product is also useful for the preparation of other compounds: Typical polysaccharides are agarose, starch, dextran, cellulose and regenerated cellulose, typical macroporous synthetic polymers are acrylamides, acrylates and methacrylates, typical rigid supports are silica beads coated with hydroxy alkyl groups and typical cabonylating agents are N,N'-carbonyl diimidazole; N,N'carbonyl di-1,2,3-benzotriazole; and N,N'-carbonyl di-1,2,4-triazole.

Abstract: Carbonylation of a polysaccharide and the product of that carbonylation. The carbonylated product can be used to prepare an affinity chromatography matrix which is an uncharged species of varying pH's. The carbonylated product is also useful for the preparation of other compounds. Typical polysaccharides are agarose, starch, dextran, cellulose and regenerated cellulose and typical carbonylating agents are N,N'-carbonyl diimidazole; N,N' carbonyl di-1,2,3-benzotriazole; and N,N'-carbonyl di-1,2,4-triazole.