60 results about "Anti proteases" patented technology

The invention provides a SOD gene from animal and a method for cloning and expressing the SOD gene in colibacillus and yeast cells, wherein a nucleotide sequence of superoxide dismutase is shown as SEQ NO.1; an amino acid sequence of the superoxide dismutase is shown as SEQ NO.2; carriers of nucleotide molecules are colibacillus plasmids or yeast plasmids; cells of the nucleotide molecules are formed by carrier conversion; and cells of the nucleotide molecules of the superoxide dismutase contain colibacillus containing the nucleotide molecules or converted by the carriers or pichia yeast containing the nucleotide molecules or converted by the carriers. The invention can prepare recombinant production strains which can efficiently express and secrete Cu/Zn-SOD, realizes the production industrialization of the Cu/Zn-SOD, and achieves good pH stability, favorable thermal stability and Cu/Zn-SOD products with anti-protease hydrolyzation capacity.

The invention relates to the field of genetic engineering, in particular to an acidophil Beta-glucanase GLU7A and gene and application thereof. The invention provides a glucanase GLU7A from acidophil bispora Bisporasp, and the amino acid sequence thereof is shown as SEQIDNO.1, and the invention provides a genome of coding the glucanase and cDNA coding gene glu7A. The invention obtains an acidophil glucanase which has the optimum pH value of 1.5-5.0, simultaneously remains high enzymatic activity in acid environment, and resists protease hydrolysis. In addition, the glucanase not only hydrolyzes Beta-1, 3-1, 4-glucanase, but also can hydrolyze cellulose. Due to the properties, the acidophil Beta-glucanase GLU7A can be applied in the industries of food, feedstuff and beer.

The invention relates to anti-VEGF polypeptides and antibody single variable domains (dAbs) that are resistant to degradation by a protease, as well as antagonists comprising these. The polypeptides, dAbs and antagonists are useful for pulmonary administration, oral administration, delivery to the lung and delivery to the GI tract of a patient, as well as for treating cancer and inflammatory disease, such as arthritis.

The invention relates to a method for selecting, isolating and/or recovering a peptide or polypeptide from a library or a repertoire of peptides and polypeptides (e.g., a display system) that is resistant to degradation by a protease such as a protease found in the GI tract or pulmonary tissue of a human. Generally, the method comprises providing a library or repertoire of peptides or polypeptides, combining the library or repertoire with a protease under conditions suitable for protease activity, and selecting, isolating and/or recovering a peptide or polypeptide that is resistant to degradation by the protease and has a desired biological activity. The selected peptides and polypeptides have utility as therapeutics, eg for treating disease or conditions of GI tract or pulmonary tissue in humans.

The invention relates to the genetic engineering field, especially to a novel gibberella Gibberela.sp. F75 with a preservation number CGMCC No.2499, and an acidic alpha-galactosidase Aga-F75 of antiprotease from said strain, further a gene thereof and a recombinant vector containing said gene. The amino acid sequence of the alpha-galactosidase Aga-F75 is shown as SEQ ID NO.1. The enzyme has a proper action pH value, a stronger protease resistance and a better hydrolysis ability for various substrates and is used for the feed and food industries as a feed or food additive agent.

The present invention relates to an antimicrobial peptide, a preparation method of the antimicrobial peptide, a composition containing the antimicrobial peptide, an antibacterial method using the antimicrobial peptide, and applications of the antimicrobial peptide. The amino acid sequence of the antimicrobial peptide is Val Pro Tyr Ile Gln His Thr Pro Asn Leu Leu Leu Glu Gln Asn LeuLeu, wherein amino acids in the amino acid sequence are all D-type amino acids. In the case, chemical synthesis is used to efficiently obtain a large amount of high-purity total reverse D-type antibacterial peptideso as to ensure the integrity and purity of the antibacterial peptide sequence, and the total reverse D-type antibacterial peptide has high thermal stability and anti-protease degradation ability. Thebroad-spectrum antibacterial activity of the total reverse D-type antibacterial peptide in this case is greatly enhanced compared with L-type antibacterial peptides.

Protease-like nucleic acid molecules and polypeptides and fragments and variants thereof are disclosed in the current invention. In addition, protease-like fusion proteins, antigenic peptides, and anti-protease-like antibodies are encompassed. The invention also provides vectors containing a nucleic acid molecule of the invention and cells into which the vectors have been introduced. Methods for producing the polypeptides and methods of use for the polypeptides of the invention are further disclosed.

The invention discloses an anti-protease 3 antibody IgG chemiluminiscence immunodetection kit. The kit comprises magnetic particles coated with a protease 3 antibody, acridinium ester coated with a mouse anti-human IgG monoclonal antibody, an anti-protease 3 antibody IgG calibration product, a pre-exciting solution and an exciting solution. The invention further discloses a preparation method of the anti-protease 3 antibody IgG chemiluminiscence immunodetection kit. Compared with an existing kit, the kit has the advantages of being easy and convenient to operate, high in sensitivity, wide in detection range and the like.

The invention relates to a protein deacetylase and proteasome double-target inhibitor, and a pharmaceutically acceptable salt, a stereoisomer, a preparation method and an application thereof. The compound is represented by general formula I, the compound has good histone deacetylase resisting activity, proteasome resisting activity and tumor cell proliferation resisting activity, and can be used for preparing medicines for preventing or treating related mammalian diseases caused by abnormal histone deacetylase expression or proteasome abnormality. The invention also relates to a pharmaceuticalapplication of a composition containing the compound with the structure of general formula I.

Antibody preparations with substantially homogeneous and unsialylated glycoforms, such as G0 and G2, are prepared by enzymatic treatment, expression under certain conditions, use of particular host cells, and contact with serum. These antibody preparations resist cleavage by proteases, such as papain, ficin, bromolein, pepsin, a matrix metalloproteinase, such as MMP-7, neutrophil elastase (HNE), stromelysin (MMP-3) and macrophage elastase (MMP-12), and glycosylation modification enzymes. The antibody preparations with substantially homogeneous and unsialylated glycoforms and methods of testing for glycosylation in an antibody are useful in connection with characterization of antibody properties and/or in diseases or conditions characterized by an increase in protease activity.

The invention discloses pegylated single-modified recombinant glutathione peroxidase (mPEG-GPX), and a preparation method and application of the pegylated single-modified recombinant glutathione peroxidase (mPEG-GPX) in preparation of antioxidant drugs, health care products and cosmetics, and belongs to the technical field of biology. The preparation method comprises the following step of carryingout covalent coupling on activated linear-chain monomethoxy polyethylene glycol succinimide succinate (mPEG-SS) and an amino group of recombinant glutathione peroxidase (GPX) to obtain mPEG-GPX. After GPX is modified by polyethylene glycol, the stability of the product mPEG-GPX is obviously enhanced compared with that of the GPX, the in-vivo antioxidant effect of mPEG-GPX is superior to that of the GPX, and development and utilization of mPEG-GPX health care products are facilitated; according to the obtained pegylated single-modified recombinant glutathione peroxidase, the pH tolerance, thethermal stability and the protease hydrolysis resistance of the recombinant glutathione peroxidase are improved, the circulating half-life period of the recombinant glutathione peroxidase in vivo is effectively prolonged, the stability of a drug is improved, and the drug effect is improved.

The invention relates to the field of gene engineering, in particular providing a novel antiprotease acid alpha-galactosidase AGA36 and a gene and an application thereof. The amino acid sequence of the alpha-galactosidase AGA36 is shown in SEQ ID NO.1, and the enzyme has appropriate acting pH value, strong resistance to metal ions and surfactants, strong protease resistance and better capacity for hydrolyzing various substrates, and can be applied to the feedstuff and food service industries as a feedstuff or a food additive.

The invention relates to the field of genetic engineering, specifically to high-temperature high-specific activity acidic beta-mannanase Man5A and a coding gene and application thereof. The amino acid sequence of the Man5A is represented by SEQ ID No. 1 or SEQ ID No. 2. The invention provides a novel mannanase gene; and mannanase coded by the gene has the advantages of acidity, high temperature, high specific activity, good heat resistance and good antiprotease capacity and can be used in the industries like feeds, food, medicines. With a technical scheme provided by the invention, production of mannanase with excellent properties and industrial applicability can be realized by using genetic engineering means.

The invention relates to a method for improving the structure of ACE inhibitory peptide prepared from food protein, and belongs to the biotechnology field. The method specifically includes the steps that the ACE inhibitory peptide prepared from the food protein is decomposed and identified through the technological means of ultra-filtration, gel chromatography, high performance liquid chromatography, mass spectrum analysis and the like, and an amino acid sequence of the ACE inhibitory peptide is clear and definite; then one to two amido bonds in the amino acid sequence of the ACE inhibitory peptide are replaced by groups such as -CHOH-, -COCH2- and -CH2CO- to form mimetic peptide substance of a non-peptide-bond structure; finally the mimetic peptide obtained after the structure improvement is synthesized with the organic synthesis method, and large-scale preparing is achieved. By means of the ACE inhibitory peptide improved with the method, the inhibitory activity can be well kept, the protease and peptidase degradation resisting capacity can be improved, and the biological activity can be improved.

The application relates to a method for diagnosis of an antiphospholipid syndrome (APS) in a subject, wherein presence or absence of an anti-protease-activated receptor 1 (PAR1) antibody is detected in a sample from the subject diagnosed, and wherein the presence of an anti-PAR1 antibody is indicative of the disease. Furthermore, it relates to the use of PAR1 for the diagnosis of APS, as well as to a method of removing anti-PAR1 antibodies from isolated blood of a subject upon detection of said anti-PAR1 antibodies in a sample of said patient.