716 results about "Collagen VI" patented technology

Compositions, methods, and systems are disclosed for using collagen-rich material, derived from adipose tissue, that is placed directly into a recipient along with such additives necessary to promote, engender, or support a therapeutic, structural, or cosmetic benefit. The compositions may be obtained during the course of a single surgical procedure, and may be administered to the patient immediately after adipose tissue is removed from a patient, such as within hours or days from being withdrawn from the patient.

The invention discloses a recombinant humanized collagen. Its amino acid sequence is as shown in SEQNO.3 and has 599 amino acids. The molecular weight is 55.0kDa. A preparation method of the recombinant humanized collagen comprises the following steps of: constructing a gene engineering strain for the expression of the recombinant humanized collagen to obtain a Pichia pastoris engineering strain; carrying out fermentation culture on the engineering strain, and realizing inducible expression of the recombinant humanized collagen to obtain a recombinant humanized collagen fermentation broth; and purifying the fermentation broth to obtain the recombinant humanized collagen. The humanized collagen gene Ge1 designed in the invention is a brand-new sequence which is greatly shorter than a natural humanized collagen gene (Kbp) in length. By the preparation method, operation simplification at the molecular level is realized, and the gene engineering strain fermentation production of the collagen is more easily realized. The humanized collagen gene Ge1 contains characteristics of a natural humanized collagen gene. And simultaneously, its expressed protein has excellent characteristics of a natural humanized collagen.

An injectable composition having dermal filling and tissue expanding activity comprises (1) a quantity of elastin sufficient to bring about dermal filling and tissue expansion when injected into a subject in need of dermal filling and tissue expansion, and (2) a pharmaceutically acceptable carrier. The composition can further comprise collagen, in other alternatives, the composition can further comprise hyaluronic acid, and one or more of the elastin, the collagen, and the hyaluronic acid, if present can be cross-linked, either intramolecularly or intermolecularly. The elastin, however, is the primary filler, even if collagen or hyaluronic acid are included in the composition

The use of collagen as a biomedical implant raises safety issues towards viruses and prions. The physicochemical changes and the in vitro and in vivo biocompatibility of collagen treated with heat, and by formic acid (FA), trifluoroacetic acid (TFA), tetrafluoroethanol (TFE) and hexafluoroiso-propanol (HFIP) were investigated. FA and TFA resulted in extensive depurination of nucleic acids while HFIP and TFE did so to a lesser degree. The molecules of FA, and most importantly of TFA, remained within collagen. Although these two acids induced modification in the secondary structure of collagen, resistance to collagenase was not affected and, in vitro, cell growth was not impaired. Severe dehydrothermal treatment, for example 110° C. for 1-3 days under high vacuum, also succeeded in removing completely nucleic acids. Since this treatment also leads to slight cross-linking, it could be advantageously used to eliminate prion and to stabilize gelatin products. Finally, prolonged treatment with TFA provides a transparent collagen, which transparency is further enhanced by adding glycosaminoglycans or proteoglycans, particularly hyaluronic acid. All the above treatments could offer a safe and biocompatible collagen-derived material for diverse biomedical uses, by providing a virus or prion-free product.

Two types of compositions having an eye-drop delivery system are used during or after an orthokeratology procedure to prevent or retard relaxation of corneal tissue back to the original anterior curvature of the cornea. Each composition functions independently from the others and is a different approach of preparing a stabilizing agent. The first composition is directed to a biologically compatible composition comprising fibril associated collagens with interrupted triple helices (FACITs) and/or small leucine-rich repeat proteoglycans (SLRPs). The fibril associated collagen family includes various types of collagens, such as type VI, type XX, type XII, and type XIV. The small leucine-rich repeat proteoglycans family includes decorin, keratocan, biglycan, epiphycan, lumican, mimecan, and fibromodulin. The second composition includes the enzyme found as a normal component of tissues, plasma, or epidermis, such as transglutaminase.

Collagen compositions, methods for preparing those collagen compositions, and graft compositions formed from those collagen compositions are provided. In particular, methods of isolating collagen that exhibits an enhanced rate of polymerization and enhanced microstructural and mechanical properties upon polymerization, such collagen compositions, and graft compositions formed from such collagen compositions are provided.

A collagen scaffold domain, including a collagenous or collagen-like domain, which directs self-trimerization is provided. The collagen scaffold domain can be fused to one or more heterologous domains, such as an antibody domain. Methods for generating and using the scaffold domains and fusion proteins are also provided.

The invention provides a preparation method of high-purity collagen protein sponge, and relates to a preparation method of collagen protein sponge. The preparation method of the high-purity collagen protein sponge is used for solving the problems that the collagen protein sponge prepared by using a conventional method is long in production cycle and low in yield and purity and has poor hemostasis performance. The preparation method of the high-purity collagen protein sponge comprises the following steps: step one. pretreating fresh bovine heel tendons; step two. extracting collagen protein; step three. centrifuging; step four. salting out; step five. dissolving; step six. carrying out gradient dialysis; step seven. pre-freezing; step eight. carrying out freeze drying; and step nine. sterilizing. The final product prepared by using the method has a smooth and flat surface and relatively good hemostatic performance and is uniform in pore size distribution. The product has relatively high purity (the total amount of amino acids reaches 97.73%), an obvious hemostatic effect and no abnormal taste, is safe, non-toxic, high in yield and short in time; liquid is clear without impurities; the production cycle is shortened; the whole preparation process is carried out at a room temperature; the biological activity of the collagen protein is maintained; and the application of the high-purity collagen protein sponge in clinical is improved.

The invention discloses a method for preparing collagen oligopeptide. Animal skins are taken as raw materials, and are subjected to acid and surfactant pretreatment, enzymolysis, decoloration, membrane separation and drying to form the collagen oligopeptide. The relative molecular weight of the prepared collagen oligopeptide is mainly distributed below 1,000Dalton, and preferably, the Gaussian distribution peak area percentage of oligopeptide with the relative molecular weight of less than 1,000Dalton is over 85 percent and preferably over 90 percent. The method solves the general problems that the conventional collagen products have odor, are dark yellow and the like; and the obtained collagen oligopeptide powder is white, free of odor and good in mouthfeel, has high absorptivity and penetrability and can be widely applied to the cosmetics industry, the food industry and the like.

A therapeutic composition for the protection, treatment and repair of connective tissue in mammals and a method for the treatment of connective tissue in mammals by the administration of the composition. The composition includes glucosamine and preferably chondroitin sulfate or fragments thereof. The composition optionally includes manganese ascorbate which catalyzes the production of collagen and proteoglycans from the glucosamine and chondroitin sulfate.

The invention relates to a method for preparing a collagen peptide by taking a cod skin as a material; in the method, the cod skin is selected as the material and is washed clearly by fresh water; 0.2 percent-0.5 percent mixed liquid of calcium hyduloxide and sodium hydroxide is added for dipping; then the cod skin is washed by fresh water until the pH value is neutral; after the water liquid of 0.3 percent to 0.6 percent diluted acid is added for dipping, the cod skin is washed by fresh water again until the pH value is neutral; the cod skin is cracked and is stirred and extracted in hot water for extracting a collagen; then undissolved substances are removed through filtering; the pH value of the extraction liquid of the collagen is adjusted to be neutral; under the stirring conditions, enzymes are added for carrying out zymohydrolysis and obtaining a zymohydrolysis liquid; and after the enzymes are eliminated and filtering is carried out, the powder of the collagen peptide is obtained through vacuum condensing and sponging drying. The method has the advantages of simple technique, less device investment, no environment pollution and being suitable for industrialization production. The collagen content of the powder of the prepared collagen peptide is higher; and the color, smell and biological properties are excellent. The powder of the collagen peptide can be broadly applied to the industries of health-care foods, medicines, and the like.

A method of stimulating collagen formation in a selected area of mammalian skin in which the selected area is irradiated with a source of visible or near infra-red radiation. The radiation is absorbable by intracellular chromophores to enhance cellular activity and increase collagen formation. A skin treatment device for carrying out the method of the invention is also described.

Surfaces useful for cell culture comprise a support to which is bound a CAR material, and, bound to the CAR material, an ECM protein, or a biologically active fragment or variant thereof such as elastin, fibronectin, vitronectin, laminin, collagen I, collagen III, collagen IV, and collagen VI. Also, optionally present on the surface is an active factor, preferably a polycationic polymer or a biologically active fragment or variant thereof, such as polyethyleneimine (PEI), poly-D-lysine (PDL), poly-L-lysine (PLL), poly-D-ornithine (PDO) or poly-L-ornithine (PLO). This surface is used in cell culture to promote cell attachment, survival, and/or proliferation of primary liver cells. The invention also relates to methods utilizing this surface, such as methods for attachment, survival, and/or proliferation of cells. Further disclosed is the use of the surface in cell culture with serum-free medium. Methods of screening using the surface of the invention are also disclosed.

The invention discloses a collagen polypeptide, a preparation method and application thereof. The collagen polypeptide comprises the following components in percentage by weight: 45-55 w/w% of components with molecular weight of 6500+/-100 Da, 20-25 w/w% of components with molecular weight of 1300+/-100 Da, and 25-35 w/w% of components with molecular weight of below 1000 Da. The nitrogen solubility index of the collagen polypeptide is 98.5-99.9%. The preparation method disclosed by the invention comprises the following steps: mixing the raw materials with complex enzyme A, and hydrolyzing.

Biological agents such as secretory cells are encapsulated in a hydrophilic gel made of agarose or collagen-agarose and gelatin sponge-agarose combinations. In a preferred embodiment, semi-solid beads are formed from a suspension containing collagen, agarose and secretory cells such as pancreatic islets, the collagen is polymerized to form solid, agarose-collagen beads and the solid beads are coated with agarose. Coating is preferably by rolling the solid beads in about 5-10% agarose, contacting the rolled beads with mineral oil and washing oil from the beads. Beads containing secretory cells can be transplanted into a mammal to treat a condition caused by impaired secretory cell function.

The present invention relates to a biological fermentative production technology of extracting high-calcium powder, chondroitin sulfate and collagen from animal cartilage which includes the following steps: the animal cartilage is simply broken into 5-20mm fragments, mixed with 1-4 times weight of water in the reaction kettle, heated to 100DEG C and kept for 1-2 hours to denature the proteins, then cold water is passed over into the kettle jacket to cool down the kettle to 40-50DEG C, compound enzyme in mass ratio of 1:0.001 which is mainly collagenase is then added, the mixture is stirred and hydrolyzed for 8-12 hours under the condition of 40-50DEG C, pH 7-8, bone residue that contains calcium phosphate is obtained after simple filtration through 100-meshed sieves; the filtrate is clarificated after fine filtration with filter press, then ethanol is added to the final concentration of 60-70%, chondroitin will be sedimentated, while remaining liquid is the mixture of collagen and ethanol. The sedimentated calcium phosphate is washed and dried and becomes calcium phosphate powder. The crystal sediment of chondroitin is purified by ethanol-washing. Collagen is separated after the mixture of collagen and ethanol goes through the ethanol regenerating column. This technology can produce different products with high purity from animal cartilage and solves the problems of pollution and single product of traditional technology.

The invention relates to a method for preparing fish scale collagen. The method comprises the following steps: fresh fish scales are taken as a material, undergo cleaning, drying and crushing, are soaked in NaOH solution for degreasing, and soaked in hydrochloric acid solution for deashing; the fresh fish scale is added with water of which the weight is 5 to 10 times of that of the fish scales, the pH value is adjusted to between 2 and 4 by acid solution, pepsin of which the weight accounting for the weight of the mixing solution is between 1 and 5 percent is added, the mixing solution undergoes enzymolysis at a low temperature for 4 to 10 hours, and enzyme is killed; enzymatic liquid is filtered twice to obtain extracting solutions, the extracting solutions are mixed, the mixing solution is decolored, sodium chloride of which the weight accounting for the weight of the mixing solution is between 5 and 15 percent is added into the mixing solution for overnight salting out, deposit is separated and collected, and acetic acid of which the weight accounting for the weight of the mixing solution is between 5 and 20 percent is added into the deposit for dissolution to obtain protein solution; the protein solution is dialyzed and desalted to obtain purified collagen liquid; and the collagen liquid is subjected to freeze-drying or spray-drying and micro-crushing to obtain solid particle. The method has the advantages of reasonable process, simple operation, safety, low cost, little loss of nutrient matters of the product, low ash content and high yield and purity of the collagen.

This invention discloses a method for preparing freshwater fish skin collagen. The method comprises: (1) washing fish skin, draining, cutting, and soaking in 0.001-0.2 M alkali solution containing 0.005-2% (v/v) H2O2 for 3-48 h; (2) stirring at a high speed, washing and soaking with an organic reagent; (3) extracting with acid solution (pH = 1.0-5.0) containing 0.01-2% (m/v) pepsin for 12-64 h, and filtering with 30-100 mu.m membrane, and then with 1-30 mu.m membrane; (4) adding 5 M NaCl solution into the filtrate to 0.8-2.0 M, centrifuging, dissolving the precipitate in 0.001-0.1 M acetic acid, dialyzing with distilled water, and freeze-drying to obtain white and odorless collagen solid. The collagen can be widely used in food, cosmetic and biomedical fields.