33 results about "1-aminohydantoin" patented technology

The invention is confluens protein of SARS virus S protein and N protein, and the manufacturing, application and the gene project technology, vaccine and diagnosing reductant. Through analyzing the cistine series of SARS s protein and N protein, sifts out SARS virus S protein segment with strong antigen epitope, namely the 162nd cistine to 460nd cistine, and the N protein segment of SARS virus with strong antigen epitope, anmely the first cistine to 258nd cistine. It synthesizes the new SARS virus S protein segment and N protein segment gene series, connects the two gene segments in series. Expresses the confluens protein of the two protein segments, the two are connected by glycine and serine, inserts a glycine adjoining to the frist cistine methionine of N protein segment, the confluens proteiní» length is 560 cistines.

The invention relates to the field of pharmaceutical synthesis, in particular to a method for synthesizing thymalfasin, and aims to solve the technical problems of difficulty in separation and purification, low total yield and high production cost of a conventional method. According to the scheme, the method for synthesizing thymalfasin comprises the steps as follows: a, a polypeptide fragment 1 and a polypeptide fragment 2 provided with protecting groups on side chains are synthesized; b, a C terminal of the polypeptide fragment 1 and an N terminal of the polypeptide fragment 2 are coupled, and the protecting group at the N terminal is removed to obtain polypeptide resin I; c, according to an amino acid sequence of thymalfasin, amino acids from the eleventh to the first are sequentially coupled one by one according to the order from the C terminal to the N terminal, then the protecting group at the N terminal is removed, and acetylation is performed to obtain thymalfasin resin; and d, the thymalfasin resin is subjected to acidolysis to remove the C terminal resin and all protecting groups to obtain a coarse thymalfasin product, and thymalfasin is obtained after purification. With the adoption of the method, the product yield can be greatly improved, and the synthesis cycle is shortened.

Provided is an affinity chromatography carrier in which high immunoglobulin-binding capacity and alkali resistance are maintained. Provided is an immunoglobulin-binding protein, wherein: the immunoglobulin-binding protein contains at least one modified immunoglobulin-binding domain; and the modified immunoglobulin-binding domain is a polypeptide comprising an amino acid sequence having at least one amino acid residue inserted between positions corresponding to 3 and 4 of the amino acid sequence of the B domain, Z domain, or C domain in an amino acid sequence of an immunoglobulin-binding domain selected from the group consisting of the B domain, Z domain, C domain, and variants thereof of Staphylococcus aureus protein A.

Disclosed is a modified flavine-adenine-dinucleotide-dependent glucose dehydrogenase (FADGDH) having an improved thermal stability compared to a wild-type FADGDH, which is preferably derived from a eukaryote, more preferably derived from a filamentous fungus, still more preferably derived from a bacterium belonging to the genus Aspergillus. For example, the modified FADGDH has a primary structure having the substitution, deletion, insertion or addition of at least one amino acid residue in the amino acid sequence for FADGDH depicted in SEQ ID NO:2 or 46 in the Sequence Listing.

The invention discloses a chemiluminescence enzyme immunoassay detection reagent kit for nitrofurantion, which comprises a kit body, an ELIAS plate arranged in the kit body and a reagent in the kit body, wherein each hole of the ELIAS plate is enveloped with an envelope antigen, and the envelope antigen is produced by coupling a metabolite 1-aminohydantoin (AHD) of the nitrofurantion and carrier protein; and the reagent comprises a polyclonal antibody of the nitrofurantion, a goat anti-rabbit antibody labeled by an ELIAS secondary antibody (horseradish peroxidase), a nitrofurantion series standard solution, a condensed phosphate buffer liquid, a concentrated cleaning solution, and a luminescent solution. The reagent kit has the characteristics of high sensitivity, good repetitiveness, simplicity, convenience, quickness, and accuracy; compared with the prior colorimetric ELISA method, the sensitivity can be improved by one order of magnitude; and the reagent kit is expected to play an important role in residue detection of the nitrofurantion of water for livestock raising, feedstuff, and animal derived food, such as milk samples, animal tissue samples, and urine samples.

The present invention intends to provide an IL-6R•IL-6 fusion protein and the like in which IL-6R and IL-6 are directly linked without a linker.The IL-6 receptor•IL-6 fusion protein of the present invention has a structure in which one amino acid residue constituting IL-6 receptor and one amino acid residue constituting IL-6 are directly bonded.

The invention relates to an organophosphorus pesticide degrading enzyme obtained by genetic engineering transformation. The organophosphorus pesticide degrading enzyme transformed by random mutation is generated by replacing an amino acid site of the organophosphorus pesticide degrading enzyme from pseudomonas stutzeri, and the replacing amino acid site is located at the 71st site. The organophosphorus pesticide degrading enzyme is excellent in degrading activity of chlorpyrifos and methyl to ethion and excellent in heat stability.

The invention relates to a method for producing large-grained nitrofurantoin crystals, and belongs to the field of chemical synthesis. The invention adopts a technical proposal which comprises: placing a crude product of nitrofurantoin formed by the condensation of raw materials of 5-nitrofurfural diacetate and 1-aminohydantoin, and DMF of which the weight is two times of that of the crude product of the nitrofurantion in a retort, heating the mixture to between 85 and 90 DEG C, stirring the mixture, maintaining the temperature for 10 minutes, stirring the mixture, opening a clamping sleeve, cooling the retort by cooling water for 80 to 90 minutes to between 30 and 35 DEG C, stopping stirring, standing the retort for 2.5 to 3 hours to less than 2 DEG C below zero, casting material, and washing the material with 95 percent ethanol to obtain odorless DMF. Nitrofurantoin crystals prepared by the process are larger and the granularity of 95 percent of the products is more than 80 meshes, so the process facilitates filtration and separation and contributes to the reduction of production cost.

The invention relates to an protein A domain Z derivative with a specific binding effect on an antibody and an application thereof. According to the invention, mutation of N23T and mutation of at least one amino acid residue are generated in a domain Z amino acid sequence. The derivative is obtained through a strategy of mutation of at least one amino acid residue in Helix1 and 2 in an protein A mutation domain Z. In addition, the invention also provides a preparation method for an affinity chromatography matrix by utilizing the domain Z derivative as a ligand. Compared with the affinity chromatography matrix by utilizing the domain Z derivative as the ligand, the domain Z derivative provided by the invention has higher chemical stability, and has a protein denaturation temperature in alkaline solution increased by 4 DEG C; and the synthesized affinity chromatography matrix maintains considerable antibody adsorption capacity.

A substitution mutation that improves polymerization activity of a polyhydroxyalkanoic acid synthase is identified. At least 1 amino acid residue selected from the group consisting of a histidine residue at position 17, a proline residue at position 71, a valine residue at position 131, a methionine residue at position 205, a leucine residue at position 230, and a proline residue at position 239 of a polyhydroxyalkanoic acid synthase derived from Alcanivorax borkumensis is subjected to substitution mutation with another amino acid.

The invention discloses a chemically synthesized HSV1 virus gD glycoprotein extracellular region gene fragment and expression and an application thereof, and relates to the fields of genetic engineering technology, vaccine and diagnostic reagent. By computer analysis, the invention screens out the HSV1 virus gD glycoprotein extracellular region fragment containing strong antigen epitope, totally 284 amino acids, namely from the 1st to the 284th; codons which are preferred by both eukaryon and pronucleus organism are selected; and a brand new gene sequence of the antigen epitope is chemically synthesized; the genetic engineering technology is utilized to express the gene fragment and prepare the strong antigen epitope fragment and antiserum of the HSV1 virus gD glycoprotein. The expressed HSV1 virus gD glycoprotein can be applicable to the detection of vaccine, HSV1 virus antibody or antigen and immune preparation of HSV1 virus monoclonal antibody and polyclonal antibody and the like.

The invention discloses a synthesis method of thymalfasin. The synthesis method comprises the following steps: a, synthesizing a polypeptide segment 1 and a polypeptide segment 2, which have protecting groups on side chains; b, coupling a C end of the polypeptide segment 1 and an N end of the polypeptide segment 2; then removing the protecting group of the N end to obtain polypeptide resin I; c, sequentially coupling the eleventh to the first amino acids one by one according to the sequence from the C end to the N end and removing the protecting group of the N end; then carrying out acetylation to obtain thymalfasin resin; d, removing the resin of the C end and all the protecting groups from the thymalfasin resin to obtain a thymalfasin crude product; purifying to obtain the thymalfasin. By adopting the method disclosed by the invention, the yield of the product can be greatly improved and the synthesis period is shortened.

The invention discloses a monoclonal antibody of furantoin residue marker aminohydantoin, and a preparation method and application thereof. The monoclonal antibody is secreted by a hybridoma cell AHD / 3D4 of which the collection number is CCTCC NO:C201151. The preparation method comprises the following steps: A, coupling hapten CPAHD and bovine serum albumin to obtain immunogen; B, coupling hapten CPAHD and ovalbumin to obtain coating antigen; C, preparing the monoclonal antibody from the immunogen in the step A, wherein the monoclonal antibody is secreted by a hybridoma cell strain AHD / 3D4 of which the collection number is CCTCC NO:C201151; D, coating a solid-phase carrier with the coating antigen in the step B; E, treating a sample to be detected with acid, adding benzaldehyde, performing ultrasonic derivation, extracting with ethyl acetate, taking nitrogen gas at the ethyl acetate layer, performing blow-drying, purify n-hexane, and redissolving a sample diluent to obtain a substance to be detected; and F, performing ELISA (enzyme-linked immunosorbent assay) detection on the substance to be detected. The invention also discloses application of a kit in furantoin residue detection of animal edible tissues. The method is convenient, quick, sensitive and accurate, and can be used for developing an ELISA kit capable of detecting 1-aminohydantoin residue in animal edible tissues.

The invention discloses a hybridoma cell strain for secreting an anti 1-amino-hydantoin monoclonal antibody and application of the hybridoma cell strain, and belongs to the technical field of biologics. The hybridoma cell strain is named a hybridoma cell strain 2G9A3-35H11, and the preservation number is CCTCC NO: C2015141. According to the hybridoma cell strain, a conjugate formed by AHD-CP (1-Aminohydantoin Hydrochloride-4-Carboxyphenyl Oxime) and bovine serum albumin is adopted as antigen to immunize BALB / c mice, spleen cells obtained after immunization are fused with rejuvenated SP2 / 0 myeloma cells, cell culture is performed with a culture medium without antibiotics, and thus the hybridoma cell strain is prepared through multiple times of screening and cloning; in in-vitro culture, the hybridoma cell strain can secrete a great number of specific antibodies of an anti-AHD derivatization product, and thus the hybridoma cell strain can be applied to rapid and accurate immunodetection and immunoassay on macrodantin metabolin.

The invention discloses a chemosynthetic HSV2 virus gD glycoprotein extracellular region gene segment as well as expression and application thereof, which relates to the technical field of gene engineering and the fields of vaccines and diagnosing agents. In the invention, through computer analysis, an HSV2 virus gD glycoprotein extracellular region segment containing strong antigen epitope is screened, and the HSV2 virus gD glycoprotein extracellular region segment contains 286 amino acid from the 1st amino acid to the 286th amino acid, and codons favored by both eucaryon and procaryote are selected to chemically synthesize a new gene sequence with the strong antigen epitope. Therefore, the gene segment is expressed by using the gene engineering technology, and the strong antigen epitope segment of HSV2 virus gD glycoprotein and antiserum of the HSV2 virus gD glycoprotein are prepared. The expressed HSV2 virus gD glycoprotein can be used for detecting vaccines, HSV2 virus antibody or antigen and preparing anti-HSV2 virus mono-antibody, poly-antibody and the like for immunity.

The invention provides a desalting method for 1-aminohydantoin hydrochloride in the field of chemical purification. The invention adopts a technical proposal that: acetone is used to treat a crude product of 1-aminohydantoin hydrochloride produced with raw materials of acetone semicarbazone hydantion, methyl sodium and ethyl chloroacetate to produce acetone semicarbazone-1-amino hydantion which is heated for circumfluence in a water solution of hydrochloric acid of which the pH value is equal to 1 to 2 to produce desalted 1-aminohydantoin hydrochloride. The content of sodium chloride in the purified 1-aminohydantoin hydrochloride is below 0.5 percent, so that salt content is lowered significantly, the quality of the sequentially synthesized drug is improved, and the production cost is decreased.

Herein disclosed are bioactive peptides and proteins having immunomodulating and antiviral activity, more particularly histidine-rich bioactive peptide complexes having the following structural formula (SEQ ID NO: 23):wherein: X1 is absent or contains not less than 1 amino acid and R1 and R2 are peptide chains containing the amino acid residues His or Cys, that interact with transition metal ions. Whereas R1 may contain up to 5 amino acid residues or alternatively be absent, R2 contains up to 3 amino acid residues or is alternatively absent. Such peptide complexes, primarily alloferon family peptides with Zn ions, enable the design of drugs based on an understanding of drug target structure and thus enable the creation of drugs with targeted mechanism of action.

The present invention discloses a single-chain antibody of an anti-schistosome monoclonal NP11-4 as well as a preparation method and application thereof, and relates to the field of gene engineering and the field of therapeutic drugs against schistosomiasis. The invention is to use a monoclonal antibody NP11-4 located at adult membrane, cercaria memberane, schistosomulum membrane, egg shell and miracidium in egg of Schistosoma japonicum, extract total RNA of hybridoma cells through a gene engineering technology, adopt RT-PCR for proliferation of genes VH and VL, and use overlap-extension PCR to connect the genes VH and VL into a single-chain antibody gene in the form of VH-linker-VL, which is subsequently connected with a pBAD / gIIIA carrier and cloned into Top10F'of Escherichia Coli to induce a soluble expression of the target gene. The zone from amino acid No.1 to No. 122 of the expressed single-chain antibody of the anti-schistosome monoclonal NP11-4 is a heavy chain gene repertoire of the single-chain antibody (VH), and the zone from the amino acid No.141 to No.254 is a light chain gene repertoire (VL) of the single-chain antibody, wherein the linker between the heavy and light chain gene repertoires consists of 18 amino acids including repeated glycines and serines, and the single-chain antibody has 254 amino acids in full length.

The invention relates to a G protein competitive inhibitory peptide, which starts from a 55 peptide sequence and obtains a series of derived polypeptides by deleting amino acid residues in any number more than one in any point from the first amino acid residue at the amino end and at least remaining twelve amino acid residues at the amino end. The length of the polypeptide is shortened up to 78.2 percent; and the polypeptide has a remarkable effect on anti-myocardial remodelling. The invention also relates to a method for preparing the series of derived polypeptides, which successfully synthesizes a target polypeptide with the purity up to 99.2 percent by utilizing advanced peptide synthesis technology. The invention further relates to the preparations containing the polypeptides and the application thereof in the preparation of an anti-myocardial remodelling medicament.

Interferon-alpha (IFNα) analog proteins modified by chemical attachment of at least one hydrophilic polymer moiety, such as polyethylene glycol chain, are described. In one embodiment, the IFNα analog protein has an amino acid sequence that differs from a native human IFNα interferon-alpha by one or more amino acid residues in the N-terminal region, comprised of between about residues 1-27, inclusive, by one or more substitutions selected based on the amino acid residue at the corresponding position of a mature interferon-tau (IFNτ) protein. Methods of treating viral diseases and other disorders with the polymer-modified IFNα analog protein are also described.

A substitution mutation that improves polymerization activity of a polyhydroxyalkanoic acid synthase is identified. At least 1 amino acid residue selected from the group consisting of a histidine residue at position 17, a proline residue at position 71, a valine residue at position 131, a methionine residue at position 205, a leucine residue at position 230, and a proline residue at position 239 of a polyhydroxyalkanoic acid synthase derived from Alcanivorax borkumensis is subjected to substitution mutation with another amino acid.

The invention relates to an organophosphorus pesticide degrading enzyme obtained by genetic engineering transformation. The organophosphorus pesticide degrading enzyme transformed by random mutation is generated by replacing an amino acid site of the organophosphorus pesticide degrading enzyme from pseudomonas stutzeri, and the replacing amino acid site is located at the 71st site. The organophosphorus pesticide degrading enzyme is excellent in degrading activity of chlorpyrifos and methyl to ethion and excellent in heat stability.

The invention discloses a monoclonal antibody NP11-4 chimeric Fab antibody against schistosoma japonicum, a preparation method and the application thereof, which relates to genetic engineering technology and the field of preparing therapeutic drugs for schistosomiasis. The application is located on the monoclonal antibody NP11-4 of surface membrane of adult worms, cercaria membrane, schistosomulum membrane, egg shell and miracidium membrane of the schistosoma japonicum; genetic engineering technology is used for extracting the total RNA of a hybrid tumor cell strain; an RT-PCR method is used for amplifying VH and VL genes; PCR is used for respectively amplifying the Fd and the total length L of murine VH, VL and human CH1of IgG1, CL, and then the chimeric Fab gene is amplified by overlapping and extending PCR and using Fd and L genes as templates; the chimeric Fab gene is restricted enzyme and connected with a carrier pComb3XSS and cloned to colon bacillus Top10F', and then an interest protein is induced to acquire soluble expression. At the N end of the expressed monoclonal antibody NP11-4 chimeric Fab antibody against schistosoma japonicum, the part from the first amino acid to the 215th amino acid is the L chain of the chimeric Fab antibody, and the part from the 216th amino acid to the 488th amino acid is the Fd section of the chimeric Fab antibody, the L chain and the Fd section are connected through a disulfide linkage, and the chimeric Fab antibody has an overall length of 488 amino acids.

The invention discloses a detection method for 1-aminohydantoin hydrochloride in animal tissues and a detection card. The detection card and a reagent are provided, wherein the surface of the detection card is provided with a colloidal gold test strip; the inner side of an ELIASA hole is provided with a monoclonal colloid gold marker antibody of frozen 1-aminohydantoin hydrochloride; the top of the surface of the detection card is provided with comparison color blocks at equal intervals; the reagent comprises deionized water, 1M hydrochloric acid, a derivatization reagent, an extraction agent, 1M sodium hydroxide, gold chloride, double distilled water, a chloroauric acid solution, a 1-percent sodium citrate aqueous solution, 0.1mol / L K2CO2 and a 0.1mol / L HCL cloning solution. In the detection method, the monoclonal colloid gold marker antibody is used, so that covalent bonds between gold particles and antibody molecules are avoided in the monoclonal colloid gold marker antibody, and the metal particles and the antibody molecules are combined through Van der Waals force among charges of different polarities; the colloid gold marker has very small influences on the specificity and affinity of the antibody, so that the detection accuracy of the 1-aminohydantoin hydrochloride can be increased.

An object of the present invention is to provide a method of efficiently constructing a gene delivery carrier having a favorable activity and expression efficiency of a protein expressed by a gene introduced by transformation. Moreover, an object of the present invention is to provide a pharmaceutical composition comprising a gene delivery carrier constructed by the construction method and a therapeutic agent for solid tumor comprising the resistant bacterium. The objects of the present invention have been attained by a gene delivery carrier consisting of an anaerobic microorganism capable of growing in a tumor tissue in an anaerobic environment and capable of expressing (A) a protein having an antitumor activity or (B) a protein having an activity of converting an antitumor substance precursor to an antitumor substance, wherein DNA encoding the protein of interest is allowed to further comprise, on the 5′-terminal side thereof, a DNA fragment comprising a nucleotide sequence encoding a peptide consisting of an amino acid sequence from the 1st to at least 4th amino acids at the N-terminus of a histone-like DNA-binding protein.