31 results about "Protein stabilization" patented technology

An osmolyte composition comprising 4 M glycerol and 4M urea for stabilizing previously transient protein folding intermediates as long-lived stable forms. A method to search for other possible stabilizing osmolyte mixtures using a screening array is also provided. These additional osmolyte mixtures may complement or augment the successful 4M glycerol / 4 M urea mixture.

The present invention is directed to stabilizing Bone Morphogenetic Protein in various lyophilized formulations and compositions. The present invention comprises formulations primarily including trehalose as an excipient for lyophilized compositions and their subsequent storage and reconstitution, and can also optionally include other excipients, including buffers and surfactants.

A strategy to improve protein stability by domain insertion. TEM 1 beta-lactamase (BLA) and exo-inulinase, as model target enzymes, are inserted into a hyperthermophilic maltose binding protein from Pyrococcus furiosus (PfMBP). Unlike conventional protein stabilization methods that employ mutations and recombinations, the inventive approach does not require any modification on a target protein except for its connection with a hyperthermophilic protein scaffold. For that reason, target protein substrate specificity was largely maintained, which is often modified through conventional protein stabilization methods. The insertion was achieved through gene fusion by recombinant DNA techniques.

Interferon-β protein analogs in which the asparagine at position 25, numbered in accordance with native interferon-β, is deamidated exhibit a biological activity of native human interferon-β at an increased level and do not require HA for protein stabilization. The deamidated product is suitable for large scale manufacturing for incorporation in HA-containing or HA-free therapeutics for treatment of diseases including multiple sclerosis. An endoproteinase-C peptide map technique that produces a fingerprint profile for proteins using an enzymatic digest followed by RP-HPLC is also useful in quality control as an ID and / or quantitative test for the deamidated products.

The invention discloses a preparation method of low-fluorine Euphasia superb protein base stock. The preparation method comprises the following steps of: 1, low-temperature autolysis: homogenizing fresh and alive Euphasia superb and treating through ultraviolet irradiation to realize autolysis; 2, protein extraction: adding water into homogenate, stirring and extracting, carrying out centrifugal separation to obtain an upper-layer liquid phase and precipitates; 3, protein stabilization: refrigerating the upper-layer liquid for storage or drying the upper-layer liquid before refrigerating the upper-layer liquid for storage; 4, protein preparation: thawing the refrigerated upper-layer liquid; adjusting pH value to 4.8-5.8 or heating for 10-30 minutes at 80-100 DEG C and then centrifuging to obtain precipitate products and carrying out spray drying to finally obtain the Euphasia superb protein base stock. The preparation method is simple to operate and is quite suitable for field operation on a fishing ship; through adoption of the preparation method, the protein recovery rate is up to 46%-51% and the fat recovery rate is up to 54%-60%; and in the prepared low-fluorine Euphasia superb protein base stock, the protein content is 70-78% / 100g of dry base stock, the fat content is 25-31g / 100g of dry base stock and the fluorine content is lower than 1.5 mcg. / g of dry base stock.

The present invention provides methods and compositions for protein stabilization, particularly the stabilization of polymerases in aqueous solutions with cationic surfactants. The present invention further provides cationic surfactants, including polyethoxylated amines, that stabilize thermostable and thermolabile enzymes in solution. These surfactants stabilize the activity of various enzymes, including thermostable DNA polymerases, thermolabile DNA polymerases and reverse transcriptases.

An electrospinning approach is disclosed for generating a dissolvable formulation of a reagent of interest in a nanoscale fiber medium. In one embodiment, the nanoscale fibers can incorporate and stabilize biological agents of interest, such as for storage at room temperature for extended periods. In one implementation, the fibers can be produced in a continuous manner and dissolve rapidly.

Provided are storage containers for proteinaceous pharmaceutical compositions which are characterized in, among other things, comprising (i) a wall portion, wherein an inner wall material thereof is selected from silica-coated glass, silicone-coated glass, polymers of non-cyclic olefins, cycloolefin polymers and cycloolefin / linear olefin copolymers and (ii) one or more closure portions not constituting part of the wall portion, and which contains a formulation of a protein. Also provided are new methods of storing proteinaceous compositions. In one aspect, the stored protein is characterized as having an amino-terminal gamma-carboxyglutamic acid (Gla) domain with 9-12 Gla residues.

Provided are storage containers for proteinaceous pharmaceutical compositions which are characterized in, among other things, comprising (i) a wall portion, wherein an inner wall material thereof is selected from silica-coated glass, silicone-coated glass, polymers of non-cyclic olefins, cycloolefin polymers and cycloolefin / linear olefin copolymers and (ii) one or more closure portions not constituting part of the wall portion, and which contains a formulation of a protein. Also provided are new methods of storing proteinaceous compositions. In one aspect, the stored protein is characterized as having an amino-terminal γ-carboxyglutamic acid (Gla) domain with 9-12 Gla residues.

Interferon-ss protein analogs in which the asparagine at position 25, numbered in accordance with native interferon-ss, is deamidated exhibit a biological activity of native human interferon-ss at an increased level and do not require HA for protein stabilization. The deamidated product is suitable for large scale manufacturing for incorporation in HA-containing or HA-free therapeutics for treatment of diseases including multiple sclerosis. An endoproteinase-C peptide map technique that produces a fingerprint profile for proteins using an enzymatic digest followed by RP-HPLC is also useful in quality control as an ID and / or quantitative test for the deamidated products.

This invention is a method of using a class of excipients for protein formulation to reduce and / or eliminate protein aggregation in solutions or solids. This class of compounds contains carbonyl group(s) to form Schiff base(s) with amino groups of proteins and also contains moieties to keep protein molecules spatially separated. This method has never been disclosed anywhere in the literature.

The invention provides a vaccine adjuvant, which includes aluminum gel, levamisole or derivatives thereof, and polyacrylic acid salt. The invention also discloses the vaccine composition containing the adjuvant and its application. The adjuvant can not only be used as an adjuvant for inactivated vaccines, but also be used to prepare protein stabilization solution. The vaccine composition containing the adjuvant can not only make the body produce humoral immunity but also produce cellular immunity, and can also produce a better immune response when the antigen content is low and a single immunization; it can also make the protein stable without degradation or irreversibility Variety.

There is provided a protein stabilizer for stably storing a protein in a solution. The protein may be an enzyme, an antibody, an enzyme-labeled antibody, or the like for a biochemical assay, etc. There is further provided a protein stabilization reagent comprising a protein-containing solution and the protein stabilizer dissolved therein. The protein stabilizer comprises a copolymer prepared by copolymerizing a monomer (a) of the following formula (1), a monomer (b) of the following formula (2), and a monomer (c) of the following formula (3).

The present invention relates to the technical field of stabilizing proteins, in particular to the therapeutic aspects of protein stabilization. L-carnitine is a useful agent for stabilizing proteins, and in a particularly favourable aspect in proteins used in the medical field. In a preferred aspect, L-carnitine is used for protecting chaperone activity, and in the medical field for preserving the activity of altered chaperone proteins. In connection with this invention L-carnitine is used for the preparation of a medicament for the treatment of diseases due to altered chaperone proteins, such as eye diseases, in particular cataract.

An osmolyte composition comprising 4 M glycerol and 4M urea for stabilizing previously transient protein folding intermediates as long-lived stable forms. A method to search for other possible stabilizing osmolyte mixtures using a screening array is also provided. These additional osmolyte mixtures may complement or augment the successful 4M glycerol / 4 M urea mixture.

The invention provides a compound containing a disulfide bond and its use and preparation method. The general structural formula of the compound is: . Wherein, said A is a substituted or unsubstituted hydrophilic monosaccharide group, oligosaccharide group, or ammonium ammonium salt group, and said B is a hydrophobic aliphatic group within 40 carbon atoms. In the present invention, by introducing a disulfide bond at the corresponding position of the small molecule, it not only retains the film dissolution and protein stabilization effect equivalent to or even better than that of the original detergent, but also can completely realize the In situ degradation, degraded into two thiol fragments, losing the properties of surfactants. With the aid of the compound, it can be used to prepare and study membrane proteins.