Abstract: A solution for extracting substantially pure RNA from a biological sample is disclosed. The solution for extracting RNA from a biological sample containing RNA and at least DNA comprises: (a) phenol in an amount of more than 50% by volume based on the total amount of the solution; (b) a polyol in an amount of 3 to 10% by volume based on the total amount of the solution; (c) a guanidinium salt at a concentration of 0.5 to 2.0 M based on the total amount of the solution; (d) a thiocyanate at a concentration of 0.1 to 0.5 M based on the total amount of the solution; and (e) a buffer for maintaining the pH of the solution at 4 to 6.

Abstract: A solution for extracting substantially pure RNA from a biological sample is disclosed. The solution for extracting RNA from a biological sample containing RNA and at least DNA comprises: (a) phenol in an amount of more than 50% by volume based on the total amount of the solution; (b) a polyol in an amount of 3 to 10% by volume based on the total amount of the solution; (c) a guanidinium salt at a concentration of 0.5 to 2.0 M based on the total amount of the solution; (d) a thiocyanate at a concentration of 0.1 to 0.5 M based on the total amount of the solution; and (e) a buffer for maintaining the pH of the solution at 4 to 6.

Abstract: Herein is reported a method for producing a polypeptide in monomeric form comprising the following step: recovering the polypeptide in monomeric form from an ion exchange chromatography material by applying a solution comprising a non-ionic polymer and an additive.

Abstract: In invention relates to a method for the isolation of RNA from tissue pretreated with formaldehyde comprising homogenizing the sample in the presence of a guanidinium salt in aqueous solution, and incubating the sample in the presence of 0.1 M to 5 M ammonium salt at a temperature between 50° C. and 100° C. The heat treatment in the presence of an ammonium salts demodifies RNA by reverting methylol groups which are formed in the presence of formaldehyde between amino groups in nucleobases of RNA and in basic amino acids, and by cleavage of methylene bridges between amino groups in nucleobases of RNA and basic amino acids, to provide high RNA recoveries and consistently high quality of RNA for further reaction, e.g. for reverse transcriptase-polymerase chain reaction or microarray analysis.

Abstract: Among other things, in general, a two-stage filtration and extraction assembly is described, as well as methods of use thereof.

Abstract: The present invention relates to a method for selectively removing virus and/or virus DNA from a solution comprising a target protein, whereby acetone is used as a precipitation agent to precipitate virus and/or virus DNA as well as the target protein.

Abstract: The invention provides methods and apparatus for the selective isolation of phosphorylated and glycosylated proteins and their fragments. Metal cation is used to precipitate proteins or protein fragments containing phospho groups and/or glyco groups. The sample preparation method can be used for several types of biological samples, including HeLa cells, food, and human cerebrospinal fluid. The proteins are isolated, recovered and ready for analysis by mass spectrometry or other analytical methods allowing detection limits down to the femtomole level. The method and apparatus are valuable tools in the field of protein analysis and diagnostics.

Abstract: A method for the production of hydrolyzed allergens from allergens comprising the steps of: a) extracting a source of allergens comprising allergenic proteins to form an extract, b) purifying the extract to remove non-protein components to form a purified extract, c) denaturing the purified extract with a first denaturing agent to form a purified denatured extract, d) refining the purified denatured extract to remove impurities to form a refined denatured extract, e) denaturing the refined denatured extract with a second denaturing agent to form denatured allergen mixture, and f) hydrolyzing the denatured allergen mixture to form the hydrolyzed allergens.

Abstract: The invention provides methods of preparation of lipoproteins from a biological sample, including HDL, LDL, Lp(a), IDL, and VLDL, for diagnostic purposes utilizing differential charged particle mobility analysis methods. Further provided are methods for analyzing the size distribution of lipoproteins by differential charged particle mobility, which lipoproteins are prepared by methods of the invention. Further provided are methods for assessing lipid-related health risk, cardiovascular condition, risk of cardiovascular disease, and responsiveness to a therapeutic intervention, which methods utilize lipoprotein size distributions determined by methods of the invention.

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: The present invention relates to a selectively soluble polymer capable of binding to a desired molecules in an unclarified mixture containing various biological materials and the methods of using such a polymer to purify a molecule from such a mixture. The polymer is soluble in the mixture under a certain set of process conditions such as pH or temperature and/or salt concentration and is rendered insoluble and precipitates out of solution upon a change in the process conditions. The polymer is capable of binding to the desired molecule (protein, polypeptide, etc) and remains capable of binding to that molecule even after the polymer is precipitated out of solution. The precipitate can then be filtered out from the remainder of the stream and the desired biomolecule is recovered such as by elution and further processed.

Abstract: A method for isolating crystals of perforin including the step of: crystallising perforin from solution at pH 6.4 to 8.0 and 20±5° C.

Abstract: A novel canola protein product consisting predominantly of 2S canola protein and having improved solubility properties, has an increased proportion of 2 S canola protein and a decreased proportion of 7S canola protein, and a protein content of less than about 90 wt % (N×6.25) d.b. The novel canola protein isolate is formed by heat treatment or isoelectric precipitation of aqueous supernatant from canola protein micelle formation and precipitation, to effect precipitation of 7S protein which is sedimented and removed.

Abstract: The invention relates to soluble selenium compositions and methods of production, separation and purification thereof. In particular the present invention provides methods of preparing water soluble selenoglycoproteins (e.g., via extracting selenoglycoproteins from selenium enriched yeast), methods of supplementing a selenium deficient composition via admixing water soluble selenoglycoproteins with the selenium deficient composition, compositions comprising the water soluble selenoglycoproteins and methods of administering the same.

Abstract: The invention describes compositions and method useful for the crystallization of membrane proteins.

Abstract: The invention provides methods of preparation of lipoproteins from a biological sample, including HDL, LDL, Lp(a), IDL, and VLDL, for diagnostic purposes utilizing differential charged particle mobility analysis methods. Further provided are methods for analyzing the size distribution of lipoproteins by differential charged particle mobility, which lipoproteins are prepared by methods of the invention. Further provided are methods for assessing lipid-related health risk, cardiovascular condition, risk of cardiovascular disease, and responsiveness to a therapeutic intervention, which methods utilize lipoprotein size distributions determined by methods of the invention.

Abstract: The present invention relates to a method for precipitation of peptide where the mixing step of the peptide with the precipitation aid and the precipitation itself are specially separated.

Abstract: The invention provides methods and apparatus for the selective isolation of phosphorylated and glycosylated proteins and their fragments. Metal cation is used to precipitate proteins or protein fragments containing phospho groups and/or glyco groups. The sample preparation method can be used for several types of biological samples, including HeLa cells, food, and human cerebrospinal fluid. The proteins are isolated, recovered and ready for analysis by mass spectrometry or other analytical methods allowing detection limits down to the femtomole level. The method and apparatus are valuable tools in the field of protein analysis and diagnostics.

Abstract: Provided are new methods for precipitating proteins comprising (a) providing a protein solution, (b) adding a salt to the solution, (c) either (i) adjusting pH of the composition to below the pI of the protein (in cases where the method is directed towards precipitation of most or all proteins in the solution) or (ii) adjusting the pH of the composition to above the pI of the protein (in cases where keeping the target protein in solution is desired), and (d) adding an organic compound to the solution, wherein (I) in the case where the method comprises step (c)(i) a two phase solution is formed wherein at least about 75% of the protein is contained in the protein phase or (II) in the case where the method comprises step (c)(ii) the method further comprises removing precipitated impurities from the protein solution.

Abstract: The invention provides methods for isolating proteins in purified form from mixtures by precipitation with citrate. The methods are advantageous in that they effectively separate a protein from lower molecular weight contaminants, including fragments or portions of the protein. Such methods are particularly useful for purifying antibodies from mixtures containing antibody proteolytic fragments and unpaired chains.

Abstract: A composition-of-matter is provided. The composition comprising at least one antibody binding moiety capable of binding an antibody-labeled target molecule, cell or virus of interest, said at least one antibody binding moiety being attached to at least one coordinating moiety selected capable of directing the composition-of-matter to form a non-covalent complex when co-incubated with a coordinator ion or molecule.

Abstract: Method for removing and selective separating peptides and proteins from a solution by controlled crystallization.

Abstract: A simple and convenient method for concentrating a biomolecule, including protein or nucleic acid molecules, from a sample. Purified and isolated biomolecules obtained by this method. Methods for improving the specificity or sensitivity of detecting a biomolecule by concentration and/or purification or isolation of the biomolecule according to the method of the invention.

Abstract: A process suitable for processing scaled-up amounts of source material in the range of tens of kilograms for the purification of alpha-1 proteinase inhibitor (API) from a mixture of unpurified proteins is provided. More particularly, a process for the purification of API from blood plasma or from plasma fractions to obtain pharmaceutical grade API on a commercial scale is provided. The API produced by the process is highly pure (at least 90% API out of the total protein) and highly active (at least 90% active API). Pharmaceutical compositions comprising the purified API and methods of using same are also described.

Abstract: The present invention provides a method of separating lipoproteins other than high density lipoproteins from a biological fluid. The method can quickly measure HDL cholesterol with a simple configuration and without the need of providing additional complicated devices. In this method, high density lipoproteins not generating any precipitate are fractionated from low density lipoproteins, very-low density lipoproteins, and chylomicrons generating precipitates. Then the precipitates are removed not by centrifugal separation based on the conventional technology, but by filtration using a filter to separate high density lipoproteins in blood serum. A hydrophilic cellulose-mixed ester is preferable as a material for the filter, and the pore diameter is 0.8 ?m or below. When the filtering method is employed, it is possible to eliminate the complicated operations required in the conventional centrifugal separation, and to shorten the time it takes for separation of the high density lipoproteins.

Abstract: The invention provides methods for isolating proteins in purified form from mixtures by precipitation with citrate. The methods are advantageous in that they effectively separate a protein from lower molecular weight contaminants, including fragments or portions of the protein. Such methods are particularly useful for purifying antibodies from mixtures containing antibody proteolytic fragments and unpaired chains.

Abstract: The present invention relates to a method for precipitation of peptide where the mixing step of the peptide with the precipitation aid and the precipitation itself are specially separated.

Abstract: A method of preparing a coagulated plant protein fraction with a medium molecular weight of between 14 to 97, by providing fruit juice in aqueous solution; precipitating a high-molecular-weight plant protein fraction whose bulk has a molecular weight of from above 100 to 600, by adjusting an acidic pH and/or a temperature above room temperature, and mechanically separating the fraction precipitated thus; precipitating a medium-molecular-weight coagulated plant protein fraction under warm conditions by treating, at pH 2 to 7, and between 60 to 90° C., the solution obtained after separation of the high-molecular-weight plant protein fraction and mechanically separating the medium-molecular-weight coagulated plant protein fraction with a molecular weight of between approximately 14 to 97, with the bulk of the molecular weight distribution being between 20 to 60.

Abstract: A method and kit for precipitating protein from an aqueous solution consists of a quaternary ammonium cationic surfactant and a chaotropic salt, used in combination to reversibly precipitate proteins from the aqueous solution. Precipitation separates proteins that are entrapped, non-specifically, in the quaternary ammonium cationic surfactant:chaotropic salt complex as a pellet. The precipitated protein pellet is purified further by washing with an organic solvent to remove the surfactant:chaotrope complex, leaving behind pure, concentrated proteins that can be washed to purify further the protein and/or re-dissolved in whatever buffer is most suited for any successive procedure, such as analysis.

Abstract: Provided are new methods for precipitating proteins comprising (a) providing a protein solution, (b) adding a salt to the solution, (c) either (i) adjusting pH of the composition to below the pI of the protein (in cases where the method is directed towards precipitation of most or all proteins in the solution) or (ii) adjusting the pH of the composition to above the pI of the protein (in cases where keeping the target protein in solution is desired), and (d) adding an organic compound to the solution, wherein (I) in the case where the method comprises step (c)(i) a two phase solution is formed wherein at least about 75% of the protein is contained in the protein phase or (II) in the case where the method comprises step (c)(ii) the method further comprises removing precipitated impurities from the protein solution.

Abstract: The present invention discloses a method of purifying bivalent antibodies or antibody fragments that are active at both Fab sites from a source of antibodies or antibody fragments using a non-chromatographic method that includes inducing the formation of cyclic immunoglobulin aggregates by addition of multivalent hapten to a salt solution of soluble antibodies or antibody fragments, wherein the multivalent hapten possesses a linker between the two haptens effective to prevent the binding of both haptens of the ligand to the same antibody or antibody fragment.

Abstract: A method for purifying a desired heterologous polypeptide from microbial fermentation broth or homogenate in which it is produced and solubilized is described. This method involves adding to the broth or homogenate an effective amount of a solution of 6,9-diamino-2-ethoxyacridine lactate (ethacridine lactate) to precipitate host cell impurities under conditions wherein the majority of polypeptide remains soluble, and separating the desired polypeptide from the broth or homogenate. The broth or homogenate containing the ethacridine lactate and polypeptide is also disclosed.

Abstract: A method of preparing a purified, virus inactivated and virus safe antibody preparation from a starting solution comprising antibodies and contaminants, the method comprising the steps of: (a) adjusting the pH of the starting solution to about 4.6 to about 4.95 in particular to about 4.8 to about 4.95 to produce an intermediate solution; (b) adding caprylate and/or heptanoate ions to the intermediate solution and maintaining the pH at about 4.6 to about 4.95 in particular pH at about 4.8 to about 4.

Abstract: The invention provides methods of increasing yields of desired conformation of proteins. In particular embodiments, the invention includes contacting preparations of a recombinant protein with a reduction/oxidation coupling reagent for a time sufficient to increase the relative proportion of a desired configurational isomer.

Abstract: The subject invention provides a process for preparing a porous collagen matrix from connective tissue, said process comprising: a porous structure forming step to treat said connective tissue with poring agent in situ; and a washing step to remove the impurity from said porous connective tissue thereby obtaining a porous collagen matrix.

Abstract: A system and method for cleanup of biological samples from contaminants prior to spectroscopy analysis. The system includes a support configured to hold a sample including a liquid having at least one group of biological molecules with a surface of the support binding the molecules at a surface tension angle to the liquid of less than 180 degrees. The system includes an evaporator configured to evaporate liquid from the support, a solvent applicator configured to apply a solvent for dissolution of the contaminants in the sample, and a solvent removal device configured to remove applied solvent from the sample and thereby at least partially remove the contaminants.

Abstract: The present invention provides a method of separating lipoproteins other than high density lipoproteins from a biological fluid. The method can quickly measure HDL cholesterol with a simple configuration and without the need of providing additional complicated devices. In this method, high density lipoproteins not generating any precipitate are fractionated from low density lipoproteins, very-low density lipoproteins, and chylomicrons generating precipitates. Then the precipitates are removed not by centrifugal separation based on the conventional technology, but by filtration using a filter to separate high density lipoproteins in blood serum. A hydrophilic cellulose-mixed ester is preferable as a material for the filter, and the pore diameter is 0.8 ?m or below. When the filtering method is employed, it is possible to eliminate the complicated operations required in the conventional centrifugal separation, and to shorten the time it takes for separation of the high density lipoproteins.

Abstract: The invention provides methods of preparation of lipoproteins from a biological sample, including HDL, LDL, Lp(a), IDL, and VLDL, for diagnostic purposes utilizing differential charged particle mobility analysis methods. Further provided are methods for analyzing the size distribution of lipoproteins by differential charged particle mobility, which lipoproteins are prepared by methods of the invention. Further provided are methods for assessing lipid-related health risk, cardiovascular condition, risk of cardiovascular disease, and responsiveness to a therapeutic intervention, which methods utilize lipoprotein size distributions determined by methods of the invention.

Abstract: A process suitable for processing scaled-up amounts of source material in the range of tens of kilograms for the purification of alpha-1 proteinase inhibitor (API) from a mixture of unpurified proteins is provided. More particularly, a process for the purification of API from blood plasma or from plasma fractions to obtain pharmaceutical grade API on a commercial scale is provided. The API produced by the process is highly pure (at least 90% API out of the total protein) and highly active (at least 90% active API). Pharmaceutical compositions comprising the purified API and methods of using same are also described.

Abstract: The amount of lipid associated sialoprotein (LSP) in body fluids such as cerebrospinal fluid, peritoneal fluid, pleural fluid, bronchial washings, saliva and sputum samples, may be determined by a method which may be automated, involving the following steps to be performed on the sample: adding a mixture of a chlorinated lower alkyl alcohol; centrifuging to yield a substantially clear upper phase; recovering the upper phase and adding to it a protein precipitating agent; mixing the resulting admixture; recovering the resulting precipitate; washing the precipitate with saline solution; centrifuging to recover the precipitate; dissolving the precipitate in water; mixing; adding to the resulting mixture an hydrolysis agent; heating; and determining the amount of lipid associated sialoprotein present by determining the optical density of the sample.

Abstract: A method of protein precipitation, concentration and removal of non-protein agents from the protein solution wherein the protein solution is treated with a protein-precipitation agent containing an acidic agent, a salt and a precipitate forming agent. After precipitation, the protein precipitate is washed with a water miscible organic solvent agent to remove non-protein agents present in the protein precipitate.

Abstract: Methods for the production of recombinant peptides comprise fermenting cells to produce recombinant peptides. A metal salt is added to a concentrate of the fermented cells after the fermentation step, prior to peptide isolation, and the pH of the cell concentrate after the addition of the metal salt is less than or equal to 7, thereby reducing the amount of trifulsides formed in the production of the recombinant peptide, with the proviso that the production does not include conversion of formed trifulside peptide into native peptide form after the addition of the metal salt. In one embodiment, the recombinant peptide is recombinant growth hormone.

Abstract: Methods for producing biological solutions such as immunoglobulins and in particular anti-D immunoglobulin substantially free of abnormal prion protein resulting therefrom. Specifically provided are methods for aggregation of prions and depth filtration of the biological solution to capture and remove abnormal and if desired, normal prion protein. The prion protein may then be eluted from the depth filter and filter washes and concentrated sufficient for detection at limits currently required by available assays.

Abstract: A method for purifying a desired heterologous polypeptide from microbial fermentation broth or homogenate in which it is produced and solubilized is described. This method involves adding to the broth or homogenate an effective amount of a solution of 6,9-diamino-2-ethoxyacridine lactate (ethacridine lactate) to precipitate host cell impurities under conditions wherein the majority of polypeptide remains soluble, and separating the desired polypeptide from the broth or homogenate. The broth or homogenate containing the ethacridine lactate and polypeptide is also disclosed.

Abstract: A method of preparing a sample of muscle tissue and of assaying the prepared sample to determine the presence of prions in the sample is disclosed. The muscle tissue is homogenized and mixed with a complexing agent which forms a complex with a higher specific gravity than PrPSc, the complexing agent or other components of the homogenate. Gravity is then used (e.g. ultra centrifugation) to concentrate the complex and the concentrate is assayed to detect prions. The muscle tissue is preferably extracted from a muscle or group of muscles such as hind limb muscle which have a higher or more preferably the highest concentration of prions as compared to other muscle in the mammal.

Abstract: A method of preparing a collagen sponge comprises mixing air into a collagen gel, so as to obtain a collagen foam which is dried. From the dried product thereby obtained, collagen sponge is obtained by isolating parts of sponge with a chamber diameter of more than 0.75 mm and less than 4 mm, or parts with an average chamber diagonal dimension of 3 mm. The collagen sponge may be used as a material for sealing wounds, possibly with a coating comprising a fibrin glue, such as a combination of fibrinogen, thrombin and aprotinin. A device for extracting a part of a collagen foam and for degenerating another part of the collagen foam to a collagen gel is disclosed. An elongated collagen sponge having a through-going hole or bore and a flexible wall may be used for re-establishing walls in a mammalian gastrointestinal funnel or trachea system.

Abstract: The present invention relates to the purification and production of human albumin from various sources through crystallization and repeated crystallization. Basic features of the invented process include providing specific reaction conditions and precipitating reagents to maximize albumin crystallization. Solubility diagrams are utilized as the basis for process control of the invented method. The current invention specifically controls phosphate concentration, pH and temperature to precisely guide crystallization kinetics and crystal yield.

Abstract: Purification process of humanPurification process of human urinary gonadotropins of high biological activity and chemical purity absolutely free of foreign contaminating materials derived from the use of biological reagents or chromatography dyes, from crude of gonadotropins. The high biological activity and chemically pure composition of human gonadotropins obtained by this process, are used for the treatment of infertility and are selected from the group of follitropin or menotropins, having a bioactivity greater than 2500 IU/mg protein as tested by biological assay in rats, for both FSH and LH hormones for menotropins and greater than 5000 IU/mg protein for follitropin having an FSH:LH ratio about 75:1. Pharmaceutical preparations of said gonadotropins free of these contaminating materials are also comprised within the present invention.

Abstract: Method for preparing a factor VIII solution that is essentially free of viruses and essentially devoid of vWF (von Willebrand factor) and factor VIII-vWF complexes by (a) obtaining a starting factor VIII solution devoid of factor VIII-vWF complexes; and (b) filtering the solution through a hydrophilic virus filter.

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.