Abstract: The present invention provides the method of obtaining IgA and IgM antibodies from chicken egg whites. The method involves separating chicken egg whites into two fractions which contain IgA and IgM antibodies exclusively. This separation method consists of raising the volume of the egg whites using purified water, lowering the pH of said volume, filtering the IgM fraction from said volume, precipitating the IgA fraction from the remaining volume, dialyzing the IgA fraction and drying the IgA and IgM fractions.

Abstract: Disclosed is a method for refolding a protein or peptide that does not contain essential disulfides and that contains at least one free cysteine residue. Also disclosed are polymer IFN-? conjugates that have been created by the chemical coupling of polymers such as polyethylene glycol moieties to IFN-?, particularly via a free cysteine in the protein. Also disclosed are analogs of bioactive peptides that may be used to create longer acting versions of the peptides, including analogs of glucagon, glucagon-like peptide-1 (GLP-1), GLP-2, Gastric inhibitory peptide (GIP), PYY, exendin, ghrelin, gastrin, amylin, and oxyntomodulin.

Abstract: The instant invention relates to the field of protein production and purification, and in particular to compositions and processes for controlling the amount of charge variants, aggregates, and fragments of a protein of interest, as well as host cell proteins, present in purified preparations by applying particular chromatography conditions during such protein purification.

Abstract: The invention relates to a method for purifying a glycoprotein, preferably FSH or a FSH mutant, comprising the steps of subjecting a liquid containing FSH or a FSH mutant to: (1) a dye affinity chromatography; (2) a weak anion exchange chromatography; (3) a hydrophobic interaction chromatography; and (4) a strong anion exchange chromatography; which may be carried out in any order.

Abstract: The invention is related to a process for separating proteins fibrinogen, Factor XIII and biological glue from a solubilized plasma fraction and for preparing freeze-dried concentrates of said proteins comprising the steps of: chromatographic purification comprising the steps of loading an anion exchanger of weak base type with the said solubilized fraction, previously equilibrated with a buffer of a predetermined ionic strength of an alkaline pH, which allows to retain the biological glue, elution of the biological glue by increasing the ionic strength of the said buffer, and separation of FXIII from fibrinogen by addition to at least one part of the biological glue eluate of at least one chemical agent precipitating the FXIII, and recovery of the resulting purified fibrinogen containing supernatant solution, and diafiltration of the fibrinogen, biological glue and resolubilized FXIII solutions, followed by a freeze-drying of said solutions.

Abstract: The present invention relates to a process for producing immunogenic polypeptides, comprising reducing disulfide bonds and blocking the resulting free thiol group with a blocking agent. The immunogenic peptides comprise a fragment of MAGE A3.

Abstract: Provided are an N-terminal truncated L1 protein of the Human Papillomavirus Type 58, a coding sequence and preparation method thereof, and a virus-like particle comprising the protein. Uses of the protein and the virus-like particle in the preparation of a pharmaceutical composition or a vaccine are further provided. The pharmaceutical composition or vaccine is used for prevention of HPV infection and a disease caused by HPV infection.

Abstract: The present invention relates to a chromatographic method of separating biological material comprising, providing chromatographic media comprising inorganic oxide particles having an average diameter of about 2 microns or less and an average pore diameter of 300 ? or more; applying a solvent comprising said biological material to said media, wherein said biological material is reversibly bonded to said media; and eluting said biological material from said media with a solvent in less than about 2 minutes for biological material having a molecular weight of less than about 100,000 Daltons.

Abstract: Embodiments of the present invention are directed to articles of manufacture, devices, methods and apparatus for performing liquid chromatography featuring a chromatographic sorbent having one or more pentafluorophenyl groups, wherein said one or more pentafluorophenyl groups are a bonded phase on a sorbent selected from the group comprising silica, organic polymers or hybrid organic silane material and said pentafluorophenyl groups are in a mono-, bi-, and tridentate forms.

Abstract: A method for obtaining a liquid from a porous solid phase is described. The method comprises forming a liquid seal at a first end of a porous solid phase to which a liquid is bound, wherein liquid of the liquid seal is immiscible with the liquid bound to the solid phase, and applying a pressure differential across the porous solid phase to cause the immiscible liquid to move through the porous solid phase towards a second end of the porous solid phase, thereby displacing the liquid bound to the porous solid phase towards the second end and releasing this liquid from the second end. Recovery of liquid from the solid phase using such methods is increased compared with corresponding methods in which no liquid seal is formed. In preferred embodiments, the liquid used to form the liquid seal is a mineral oil. The methods have particular application in nucleic acid extractions which utilise capture of nucleic acid to a solid phase. Kits and apparatus for performing the methods are also described.

Abstract: A novel separating agent for protein purification which not only can adsorb proteins in a sufficient amount for protein purification from a low concentration buffer but also can desorb the adsorbed protein easily just by altering the pH of the buffer and a simple and economical method for its production and a method for protein purification using it. One or two ligands selected from the group consisting of a ligand represented by the following formula (1): (wherein m is an integer of from 2 to 6) and a ligand represented by the following formula (2): (wherein each of R1 and R2 is independently a hydrogen atom or a C1-4 alkyl group, and n is an integer of from 1 to 6) are immobilized on a support via a urethane bond without intervention of a spacer arm.

Abstract: The present invention pertains to a process for production of recombinant arylsulfatase A in a cell culture system, the process comprising culturing a mammalian cell capable of producing rASA in liquid medium in a system comprising one or more bio-reactors; and concentrating, purifying and formulating the rASA by a purification process comprising one or more steps of chromatography. Other aspects of the invention provides a pharmaceutical composition comprising rASA, which is efficiently endocytosed via the mannose-6-phosphate receptor pathway in vivo as well as a rhASA a medicament and use of a rhASA for the manufacture of a medicament for reducing the galactosyl sulphatide levels within target cells in the peripheral nervous system and/or within the central nervous system in a subject.

Abstract: The present invention relates to granulocyte colony stimulating factor (G-CSF) modified with Y-shaped branched polyethylene glycol (YPEG-G-CSF) at a specific lysine (Lys 17) and the preparation thereof, as well as the pharmaceutical composition comprising YPEG-G-CSF and use thereof.

Abstract: The method of the present invention comprising successive column chromatography processes for the purification of an anthrax protective antigen can achieve an improved purity of the anthrax protective antigen product by effectively removing impurities (e.g., cellular residual proteins in the culture solution) without the loss of anthrax protective antigen. Therefore, the method of the present invention can be advantageously used for economically producing the anthrax protective antigen on a large scale.

Abstract: The current invention reports a method for the purification of a non-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second c

Abstract: The invention relates to a method for extracting a protein from milk, having at least one hydrophobic pocket and a negative charge to the natural pH of milk, that comprises the following steps: a) skimming and delipidation of the milk; b) passing the delipidated and skimmed fraction containing the protein on a chromatographic substrate on which is grafted a ligand having both a hydrophobic characteristic and an ionic characteristic in pH conditions enabling the protein to be retained on the substrate, the pH being higher than 4.6; c) elution of the protein; d) purification of the eluted fraction by removing the milk proteins from the eluted fraction; and e) recovering the protein.

Abstract: The present invention provides unstructured recombinant polymers (URPs) and proteins containing one or more of the URPs. The present invention also provides microproteins, toxins and other related proteinaceous entities, as well as genetic packages displaying these entities. The present invention also provides recombinant polypeptides including vectors encoding the subject proteinaceous entities, as well as host cells comprising the vectors. The subject compositions have a variety of utilities including a range of pharmaceutical applications.

Abstract: The invention relates to a process for the removal of glycoalkaloids, in particular from process streams such as those encountered during isolation of proteins from potatoes.

Abstract: Methods for purifying human Calciviruses are disclosed, including Noroviruses and Sapoviruses.

Abstract: The present invention provides methods of purifying immunoconjugates.

Abstract: The invention includes a process for extracting a target protein from E. coli cells that includes lowering the pH of a whole E. coli cell solution to form an acidic solution, disrupting the cells to release the protein into the acidic solution, and separating the cellular debris from the released protein to obtain a protein product enriched in the heterologous target protein. The invention also includes addition of a solubility enhancer.

Abstract: A method of preparing anti-b amyloid immunoglobulin involves treating human plasma anti-b amyloid immunoglobulin under alkaline conditions, such as at pH 10.25 to 11.75 using diethylamine HCl, to dissociate b amyloid protein therefrom. Typically, the anti-b amyloid immunoglobulin is present in human immunoglobulin preparations obtained from plasma or serum. Anti-b amyloid immunoglobulin prepared by the method is substantially free of b amyloid protein and has therapeutic activity in compositions and/or methods for treating a disease or condition associated with b amyloid plaques, such as Alzheimer's disease.

Abstract: The present invention provides improved methods for the purification of factor XIII. In particular, the methods provide compositions containing 5% or less contaminating proteins. In particular embodiments of the present invention the methods provide purified factor XIII compositions comprising less than 1% activated factor XIII, less than 2% protein aggregates, and/or less than 5% charge isomers of factor XIII. The methods do not require the use a precipitation or crystallization step common to prior methods of isolating factor XIII. Instead, the method uses immobilized metal affinity chromatography to remove various contaminants common to recombinant expression of factor XIII. Further, a combination of various chromatography methods including ion exchange chromatography, hydrophobic affinity chromatography, and immobilized metal affinity chromatography comprise a simple and less expensive method to produce a pharmaceutical grade factor XIII product at high yield.

Abstract: The present invention refers to a device, comprising a hollow body having at least one open end comprising at least one solid matrix binding, adsorbing, absorbing, chelating or retaining compounds which are not desired in a sample and preferably at least one barrier which is non-permeable for liquids and solids under ambience conditions, however, becomes liquid-permeable by applying an external force to said barrier, the use of such a device for isolating or purifying a biomolecule from a sample, a method for preparation of said device and a method for isolation or purification of any biomolecule using said device.

Abstract: In large-scale purification of proteins such as antibodies, an economic high-purity purification method is required. The present invention relates to a method for purifying a protein, including one or more chromatographic processes, in which an amino acid; or a dipeptide, an oligopeptide, or a polyamino acid thereof is included in a buffer solution used in at least one chromatographic processes (equilibration buffer, wash buffer, and elution buffer), thereby purifying a high-purity protein with a very small quantity of the impurity (e.g., polymers or host cell proteins).

Abstract: During the production of recombinant proteins from gram negative bacteria, lipopolysaccharides (LPS, endotoxin) are released along with the protein of interest. In many instances, LPS will copurify with the target protein due to specific or non-specific protein-ILPS interactions. We have investigated the ability of alkanediols to effect the separation of LPS from protein-LPS complexes while the complexes are immobilized on anion or cation exchange chromatographic media. Alkanediols provide a safer alternative to the use of other organics such as alcohols or acetonitrile due to their lower toxicity and decreased flammability. In addition, they are less costly than many of the detergents that have been used for such purposes. LPS removal efficiency increased with increasing alkane chain length. 1,2-alkanediols were more effective than terminal alkanediols in the separation of LPS from protein LPS complexes.

Abstract: A method for purifying a recombinant protein using a multimodal or mixed mode resin containing ligands which comprise a hydrophobic part and a negatively charged part is described. The invention is advantageous in that it is a single step chromatographic process which does not require adjustment of pH or conductivity during loading step and results in high yield and potency. The process is used for the purification of recombinant compositions of coagulation factor, particularly recombinant Factor VIII.

Abstract: The present invention relates to compositions, methods for expressing, and related methods for purifying calreticulin that is free of an affinity label or tag (i.e., non-tagged calreticulin). The invention provides useful methods for commercial production of human calreticulin in a bacterial expression system such as Escherichia coli.

Abstract: The invention relates to a method for purifying a factor XIII polypeptide from a biological material, the method comprising subjecting the material to sequential chromatography on an anion-exchange matrix and a hydrophobic interaction matrix.

Abstract: This invention is directed to methods for removing, preferably simultaneously and in one step, multiple impurities form crude culture samples, and, in particular, the removal of media components, protein, nucleic acids, lipids, and lipopolysaccharides to ultralow levels. Preferably the purification process comprises: (1) binding of the target substance containing one or more contaminants to a chromatography matrix; (2) washing the bound target substance with one or more buffers containing a synergistic combination of a lyotropic agent or organic solvent, a detergent, and a salt component; and (3) desorbing the target substance from the chromatography matrix, so that the eluate contains ultra low levels of contaminants. The reduction of impurities that can be achieved is preferably 91-99.9% as compared to the amount of impurities in the target substance before purification. The invention is also directed to the targets products that have been so purified.

Abstract: The present invention provides a method for purification of a protein that is conjugated to an albumin binding moiety from a mixture comprising (i) said protein in said conjugated form and (ii) said protein in a form that is not conjugated to said albumin-binding moiety, the method comprising: (a) providing a solid support comprising a substance capable of specifically binding to the albumin binding moiety; (b) contacting said solid support of (a) with said mixture comprising protein and conjugated protein under suitable conditions for binding of the albumin binding moiety to the substance as defined in (a); and (c) eluting components bound to the solid support.

Abstract: The invention provides systems, methods and kits for the separation and/or purification of at least two cellular components selected from genomic DNA, RNA and proteins. The method includes first lysing a biological sample to generate an aqueous solution containing the cellular components; then applying the aqueous solution to a first mineral support under conditions for genomic DNA to bind; and collecting the flowthrough which contains unbound total RNA and proteins. The method further includes applying the flowthrough to a second mineral support under conditions for RNA to bind, and collecting the flowthrough which contains proteins. The genomic DNA and total RNA bound can be eluted while the protein in the flowthrough can be further purified. Further the total RNA isolated could be used to isolate small RNA such as microRNA.

Abstract: The present invention relates to a method for obtaining highly purified hydrophobic proteins from cells by extraction using a buffer containing a detergent and removal of said detergent by hydroxyapatite (HA) column chromatography.

Abstract: The invention is directed to a method for purifying a protein. The method involves providing a sample containing the protein, processing the sample through a capture chromatography resin, inactivating viruses in the sample, and processing through at least one depth filter and ion-exchange membrane.

Abstract: The present invention provides a method and automated system for the purification of polypeptides including the direct filtration of solutions containing the polypeptides after purification.

Abstract: The invention describes a new class of crystalline silica material having two levels of porosity and structural order. At the first level, building units are nanoslabs of uniform size having zeolite framework. At the second structural level, nanoslabs are assembled, e.g. linked through their corners, edges or faces following patterns imposed by interaction with cationic surfactant or triblock copolymer molecules. After evacuation of these molecules, microporosity is obtained inside the nanoslabs, and a precise mesoporosity between the nanoslabs depending on the tiling pattern of the zeolite nanoslabs, as evidenced by X-ray diffraction. These materials are useful for the fixation of biologically active species, such as poorly soluble drugs.

Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the dynamic capacity of the column for either single salt alone.

Abstract: A method for changing a globular protein structure into a fibrillar protein structure. The method comprising the steps of providing a globular protein, forming a solution containing the globular protein, adding a detergent to the solution containing the globular protein, applying the solution to a molecular sizing column with a pore size of at least 70 kDa and eluting with a solution containing detergent. A method for changing an unfolded protein structure into a fibrillar protein structure. The method comprising the steps of providing a globular protein, forming a solution containing the globular protein, adding a urea to the solution to unfold the globular protein, applying the solution to a molecular sizing column and eluting with a solution containing detergent. A method for treating cancer comprising the steps of providing a protein, changing the protein into a fibrillar structure, and administering a therapeutically effective amount of the fibrillar structure protein to a patient in need thereof.

Abstract: Pretreatment is performed using a pretreatment cartridge for separating substances that is packed with a stationary phase that is coated on its surface with a polymer whose tendency to hydration will change within a temperature range of 0-80° C. and which is capable of changing the affinity between the substance to be separated and the surface of the stationary phase in response to the shrinkage or swelling of the polymer chain due to temperature change. By using this pretreatment cartridge for separating substances, a convenient operation will suffice for a sample solution to be reduced to a solution containing the substance that need be separated from the specimen. If this method of pretreatment is used, useful substances can be separated intact by merely changing the temperature and it becomes possible to perform the subsequent analyzing or fraction collecting operation efficiently.

Abstract: A process is disclosed for separating biomolecules from an aqueous solution containing the biomolecules and impurities, having different affinities and/or interactions with a solid support. The solution is passed over a fixed bed of chromatographic resin containing at least three zones, with flow of liquid being arranged between adjacent zones and between a last and first zone. Each of several sequences includes at least an adsorption stage, a rinsing stage, or a desorption stage, with each subsequent sequence being carried out by a downstream displacement of fronts in the zones by approximately the same increment before the periodical displacement of the introduction and withdrawal points.

Abstract: A spin column device, which contains a rigid porous filter that retains its shape during centrifugation, chromatography methods using the device to isolate a desired substance, e.g., a biological molecule, from other substances in a mixture, and kits containing the device with one or more reagents for use in the method.

Abstract: Herein is reported a method for determining whether a re-useable chromatography column packing, which is used at least for the second time in a purification step of a purification of a polypeptide, has reduced separation efficacy in said purification step of said purification of said polypeptide, comprising the following steps: a) identifying and determining the experimental data of an inert change of at least one physicochemical parameter of a mobile phase passing through said re-useable chromatography column packing, b) determining the parameters of a function of formula I by fitting the experimental data of the inert change of the physicochemical parameter of the at least second use, c) determining the difference between the experimental data of the inert change of the physicochemical parameter of the at least second use and the function of formula I with the parameters determined in step b), d) calculating the difference between the maximum value and the minimum value of the difference determined in step

Abstract: A process for the separation of biological materials, such as dye-ligand affinity chromatography, wherein an adsorbent is used, which comprises a reaction product of certain reactive anthroquinone compounds and a substrate having a group capable of reaction with a reactive group in said reactive anthroquinone compounds to form a covalent bond.

Abstract: Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Antitrypsin (A1AT) or a combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins. A complex of all proteins found currently in Plasma, Cryoprecipitate, Fraction III and many newly found proteins now being identified or any substances which are known proteins or unknown proteins which contain GOOD HEALTHY CELLS and the combination of any of these known or unknown proteins which contain any one of these GOOD HEALTHY cells: Neutrophil, Lymphocyte, Eosinophil, Basophil, and Marcophage, and their potential applications for treating a wide variety of diseases and other physical conditions and disorders, and for maintaining health.

Abstract: Biologically active tetrameric p53 proteins and p53 fusion proteins are provided. These proteins may be generated and refolded into tetrameric form using denatured proteins produced from E. coli. Therapeutic uses of p53 proteins and p53 fusion proteins are also provided.

Abstract: There is provided a method for the identification of macromolecule targets of analytes such as drugs in biological samples comprising complex mixtures of macromolecules. A biological sample is contacted with one or more analyte and the mixture is resolved such that the analyte and its target are co-eluted and analyzed to identify analyte-target complexes.

Abstract: The present invention relates to compositions and methods for the chromatographic purification of antibodies, such as monoclonal antibodies, employing improved simulated moving bed separation strategies and, in certain embodiments, Raman spectroscopy.

Abstract: The present invention relates generally to the production, purification, and isolation of human growth hormone (hGH). More particularly, the invention relates to the production, purification, and isolation of substantially purified hGH comprising non-naturally encoded amino acids and hGH from recombinant host cells or culture medium including, for example, yeast, insect, mammalian and bacterial host cells. The process of the present invention is also useful for purification of hGH linked to polymers or other molecules.

Abstract: The present invention relates to methods for the separation of various components from eggs. More particularly, the present invention relates to methods for the separation of proteins and lipids from eggs, including technical eggs (inedible) or edible eggs, yolks or whites, which comprises cross-linking the lipids of eggs with a cross-linking reagent. In an embodiment, the method includes separating the proteins from the cross-linked lipids. In an embodiment, the method includes the separation of various components associated with the cross-linked lipids. The methods disclosed herein allow for the isolation of multiple different components from the egg in an efficient, cost-effective manner without compromising the recovery process of the components or their subsequent utility in various applications or compositions. The compositions and isolated components obtained by the methods of the invention can be used in pharmaceutical, medical, nutritional, cosmetic or health applications.

Abstract: An improved process for the purification of antibodies from human plasma or other sources is disclosed. The process involves suspension of the antibodies at pH 3.8 to 4.5 followed by addition of caprylic acid and a pH shift to pH 5.0 to 5.2. A precipitate of contaminating proteins, lipids and caprylate forms and is removed, while the majority of the antibodies remain in solution. Sodium caprylate is again added to a final concentration of not less than about 15 mM. This solution is incubated for 1 hour at 25° C. to affect viral inactivation. A precipitate (mainly caprylate) is removed and the clear solution is diluted with purified water to reduce ionic strength. Anion exchange chromatography using two different resins is utilized to obtain an exceptionally pure IgG with subclass distribution similar to the starting distribution. The method maximizes yield and produces a gamma globulin with greater than 99% purity. The resin columns used to obtain a high yield of IgG retain IgM and IgA.