125results about "Keratin" patented technology

A method of drilling or gas-lifting is disclosed where the methods including the use of a foaming agent and a gas, where the foaming agent is a keratin and the hydrostatic pressure of the fluid in the well is for a portion of the drilling or gas-lift operation less than an hyrdrostatic pressure of the formation being drilled or under production.

Combinatorially generated peptides are provided that have binding affinity for Polytetrafluoroethylene (NY). The peptides may be used to deliver benefit agents to various PTFE surfaces.

Methods are provided to produce optimal fractionations of charged keratins that have superior biomedical activity. Also provided are medical implants coated with these keratin preparations. Further provided are methods of treating blood coagulation in a patient in need thereof.

The present invention relates to provide a protein group binding to keratin which is the major component of body hair, or genes encoding the same, particularly to keratin-associated proteins (KAP) which bind specifically and strongly to hair keratin or genes encoding the same. The base sequence of eurochromtic region of approximately 33.5 Mb of human chromosome 21 was determined, a dot-matrix analysis of the base sequence of the long arm region of chromosome 21 (21q22.3) was carried out, homology search was made to low frequency repetitive sequences and 16 KAP genes being expressed only in hair root cells were found. Moreover, the high frequency repetitive sequences present in the sequence spanning for approximately 1 Mb between CLDN8 gene and TIAM1 gene in the long arm region of chromosome 21 (21q22.11) were masked, the presence or absence of short low frequency repetitive sequence was searched, and 22 KAP genes were found. Moreover, a group of functional peptide was designed from the above mentioned KAPs.

Soluble keratin derivatives are disclosed. The soluble keratin derivatives may include a soluble keratin protein having at least one substituted chemical group at a lysine group, terminal amine group and/or hydroxyl amino acid group of a soluble keratin protein. Soluble keratin derivatives may be formed by succinylation or quaternisation, or by reaction with fatty acid derivatives. The soluble keratin derivatives may be used in personal care formulations, and may also comprise mixtures of several different soluble keratin derivatives.

A process for producing a solubilized keratin of utility value easily with high yield while suppressing coloration and smelling occurring in the hydrolysis of keratin. There is provided a process for producing a solubilized keratin, characterized in that it comprises regulating the water content of keratin raw material to a hydrous state of 20 to 80%, hydrolyzing the same in an alkali solution, neutralizing the hydrolyzate liquid, and extracting a keratin hydrolyzate from the supernatant.

Methods for producing biocompatible heterogeneous proteinaceous networks crosslinked with a heterogeneous crosslinking agent, and novel heterogeneous crosslinked networks. Preferred heterogeneous crosslinking agents are silicone-based.

The invention relates to a monoclonal antibody capable of recognizing a human leukocyte differentiation antigen CK8, a secretory cell strain, a preparation method thereof and application in immunodetection. According to the technical scheme, 340-365 amino acid sequences at the C tail end of CK8 protein are selected as antigen peptides, and the antigen peptides are coupled with KLH carrier protein to obtain the immunogen; the amino acid sequence of the antigen peptide is shown as SEQID1, a mouse is immunized, and the mouse hybridoma cell strain 14C2 capable of efficiently secreting the anti-CK8 protein monoclonal antibody and the anti-CK8 protein monoclonal antibody secreted by the cell strain are obtained through cell fusion, screening and subcloning. The antibody obtained by the scheme has high specificity and sensitivity, can specifically recognize cells expressing the CK8 protein, and is suitable for immunological detection, especially immunohistochemical detection.

The invention belongs to the field of biomedicine and particularly relates to soluble human keratin and application thereof. The soluble keratin is obtained through the following process of cloning amiddle sequence of a human gene K37, constructing a recombinant vector, transforming bacteria, inducing expression of the recombinant protein and purifying the recombinant protein to obtain the soluble keratin. The soluble keratin has the characteristic of rapid swelling and can promote mitosis and migration of epidermal cells, and therefore the soluble keratin can be used for preparing biologicalmaterials or medicaments for promoting cell proliferation or migration, and plays a role in hemostasis and wound healing. Moreover, the soluble keratin causes no rejection phenomenon when being usedfor the human body, is safe to use and thus has a wide application prospect in the field of biomedicine.

The invention discloses a keratin biomacromolecular nitric oxide donor. The keratin biomacromolecular nitric oxide donor contains reduced keratin obtained through reduction treatment on keratin, and SNO groups are formed on the sulfydryl groups of the reduced keratin. The keratin biomacromolecular nitric oxide donor is an S-nitrosated keratin and is synthesized and prepared through reaction between the reduced kertin and tert-butyl nitrite or sodium nitrite. The keratin biomacromolecular nitric oxide donor is high in molecular weight, stable in storage and capable of releasing nitric oxide under certain conditions. The keratin biomacromolecular nitric oxide donor can directly serve as a nitric oxide donor as well as be compounded with other polymers to prepare nitric oxide releasing materials to give play to a controllable nitric oxide releasing function, thereby being applicable to preparing materials such as artificial blood vessels, intravascular stent and wound dressings.

Methods for chemically modifying peptides, preferably keratinaceous feedstocks, to achieve desired solubility characteristics; stable solvent systems for preparing the modified peptides; and, the resulting chemically modified peptides.

The invention relates to a wool keratin extraction method. The method comprises the following steps: 1, immersing wool in a compounded ionic liquid, adding loose wool to the compounded ionic liquid, and heating the ionic liquid under vacuum conditions to 80-100DEG C for 2h while stirring until the wool is dissolved to form a beige liquid; 2, adding the treated liquid obtained in step 2 to a buffer solution; 3, centrifuging the treated solution obtained in step 2 to obtain wool keratins; and 4, adding the buffer solution to a centrifuged liquid obtained in step 3, circulating the step 2 and the step 3, repeatedly extracting 4-10 times, and mixing all the separated wool keratins.

A hair treatment composition containing at least one peptide identical to human hair, where preferably the peptide is synthesized from naturally-derived amino acids and can serve as a natural alternative to the commonly used human or animal derived (wool) keratin peptides.

A process for separating keratinous proteins from a keratin-containing material, the process comprising the steps of: subjecting the keratin-containing material to reduction in a liquid medium to solubilise the keratinous proteins under conditions that minimise hydrolysis of the keratinous proteins, to yield a solution of keratinous proteins and undissolved solids; subjecting the solution of keratinous proteins to peroxide oxidation, without any intervening keratin precipitation step; and separating the solution of keratinous proteins from the undissolved solids prior to, at the same time as, or following the oxidation step. Preferred conditions for performing the reduction step involve contacting the keratin-containing material with a solution of an alkali metal sulfide reducing agent at a temperature of between 25 C and 50 C for a time of between 30 and 90 minutes, assuming atmospheric pressure. The peroxide oxidation is suitably carried out within not more than 4 hours after the reduction step, and involves reducing the pH of the solution to a level not less than pH 10, although pH 11.3 is most preferred. The product is demonstrated to have a principal fraction that has a molecular weight above 10 kDa, reflecting that the disulfide bonds in the keratinous proteins are broken without hydrolysis of the proteins.

The invention relates to a keratin-chitosan composite medical dressing and a preparation method thereof; the dressing is prepared from, by weight, 2-8% of keratin, 0.6-1% of sodium carboxymethyl cellulose, 0.3-0.9% of chitosan, 6-8% of glycerol, and the balance of water. The preparation method comprises: adding keratin and sodium carboxymethyl cellulose into water, adding chitosan and glycerol, mixing well, and performing first lyophilizing; soaking sequentially in CaCl2 solution and NaOH solution, and performing second lyophilizing after soaking is complete; soaking in glycerol aqueous solution, and performing third lyophilizing after soaking is complete. The keratin-chitosan composite medical dressing prepared herein has no immunogenicity, is good in hemostatic effect and high in air permeability, and also has the advantages, such as good biocompatibility and the ability to promote cell growth.

The present invention describes a method to inhibit replication of the human immunodeficiency virus (HIV) by negatively modulating or altering the cytoskeleton, more precisely the proteins forming the intermediate cytoskeletal filaments, wherein the said proteins are vimentin and/or keratin-10. The replication of the virus is inhibited in human cells by intervening in the structure of these proteins. The present invention is also related to the use of agents, which comprise peptides and/or interfering RNA and/or lipidic compounds, said agents producing a negative modulation or alteration of the cytoskeleton to prevent or to treat the HIV infection. The invention provides means and methods for altering the cytoskeleton/filament structure of cells, as a result of which the infection of human cells by HIV is disturbed and can even be completely inhibited. The cytoskeleton is altered by reducing the amount of vimentin and/or keratin (e.g. by transcriptional control using interfering RNA) or by using peptides that disrupt the cytoskeleton.

Described herein are methods to produce keratin protein-based biomaterials, the parameters required to achieve improved extraction, the parameters required to improve isolation, the parameters of lyophilization and the grinding process to achieve consistent particulate sizes of protein materials.

The invention relates to a method for extracting keratins from rabbit hair. The method comprises the following steps: 1, performing hydrogen peroxide pretreatment and drying to obtain dry rabbit hair; 2, performing enzymatic treatment and drying to obtain dry rabbit hair; 3, performing ZnCl2 treatment to obtain a solution of the rabbit hair; 4, extracting the keratins from the rabbit hair to obtain precipitates by adopting an isoelectric precipitation method; 5, flushing the precipitates for multiple times by using distilled water, and performing drying and grinding to obtain keratin powder. The method has the beneficial effects that a three-step treatment method comprising hydrogen peroxide pretreatment, enzymatic treatment and 40 percent ZnCl2 treatment is adopted, and compared with a purer ZnCl2 treatment method, has the advantages that the dissolution time of the rabbit hair is remarkably shortened, and energy consumption in an extraction process is reduced; the precipitates are washed for multiple times by using the distilled water, so that the concentration of Zn<2+> can be remarkably reduced, impurities can be reduced, and the purity of the keratins in the rabbit hair can be improved; the method is simple in process, low in treatment cost and high in rabbit hair keratin extraction rate.

The present invention provides an inhibitor of an autoimmune response to a periodontal bacterial enzymatic degradation product of keratin in gingival epithelium in a mammal having a periodontal bacterium in the oral cavity, containing a substance having affinity to the keratin or a degradation product thereof and/or a substance having affinity to an autoantibody to the degradation product, an agent for the prophylaxis and/or treatment of a periodontal disease and/or a complication thereof; a RANKL expression inhibitor containing a substance having affinity to the keratin or a degradation product thereof; and a method of diagnosing a periodontal disease including detecting the keratin or a degradation product thereof and/or an autoantibody thereto.

The invention discloses a waste feather regenerated pure keratin fiber and a preparation method thereof. The preparation method of the waste feather regenerated pure keratin fiber comprises the stepsthat performing high-temperature flash explosion treatment on waste feathers and then performing treatment with urea to obtain feather keratin; dissolving the feather keratin, and adding an antibacterial agent while dissolving; adding sodium hexadecyl sulfonate, performing aging, and heating to obtain a spinning solution; and preparing the regenerated keratin fibers by using the spinning solution.The waste feather keratin with excellent molecular weight and yield is obtained by adopting a high-temperature flash explosion and low-concentration urea synergistic treatment method, the antibacterial regenerated keratin fibers with high additional values are developed on the basis, a new solvent system of sodium carbonate, sodium bicarbonate and hexadecyl sodium sulfonate is developed, and thespinnability of a keratin solution is improved.

The present invention relates to a method for preparing an ultra-low-molecular-weight keratin peptide and a use thereof. In particular, the present invention relates to: an ultra-low-molecular-weightkeratin peptide preparation method using the cultivation of microorganisms having keratin decomposition activity in a culture medium including keratins, ultrafiltration, ion exchange chromatography, and gel filtration chromatography; a peptide prepared according to said method; and cosmetic and food compositions for preventing or reducing skin aging or skin wrinkles, comprising said peptide. The keratin peptide preparation method according to the present invention enables environmentally friendly biological treatment of waste resources and effective refinement and recovery of an antiaging, functional, ultra-low-molecular-weight keratin peptide. In addition, the keratin peptide according to the present invention has inhibitory activity against the expression and activity of MMP-1, which isan enzyme that causes skin aging by decomposing collagen, thus has excellent effects of preventing skin aging and reducing skin wrinkles, is appropriate for use as cosmetic, pharmaceutical, and food compositions for preventing, reducing, or treating skin aging and skin wrinkles by having no toxicity to skin cells, and thus can be usefully used for efficient and quick production and development ofhigh value-added functional cosmetic materials.