The method of producing immunoglobulin for intravenous administration and its variants
(57) Abstract:The invention relates to medicine, namely to produce preparations of intravenous immunoglobulins from human blood. The essence of the invention is that as the initial solution using the filtrate III, who concentrated by ultrafiltration at pH 3.8 to 4.5, followed by diafiltration against distilled water, the treatment with pepsin and removing the aluminum hydroxide is carried out in the presence of sugars and chloride content less than 0.2%, then enter glycine, set the amount of pH 4.0-7.5, the protein content of 4.5-5.5 percent, physiological NaCl received the drug for choice later use in liquid or dry form. Alternatively pepsin can be removed by ultrafiltration or dialysis, or anion exchange chromatography, the desired product may have a pH value of 4.0 to 4.5, and a dry form of the drug must contain additional stabilizer - maltose. The advantage of the invention is to improve the quality of the target product, the simplification and the reduction of the technological cycle of production of the drug, increasing the shelf life of the target product. 2 S. and 4 C. p. F.-ly, 3 tables. The invention Rel-Christ. Preparations of immunoglobulins are used for treatment and prevention of various infectious diseases and immunodeficiency diseases. Currently, preparations of immunoglobulins prefer to be given intravenously, which allows to achieve maximum effectiveness in the short term.Intravenous administration of immunoglobulin is associated with side effects, the most important of which is the activation of the complement system, accompanied by severe reaction, in some cases, collapse. Adverse reactions can be caused by the presence in the product of the aggregated and damaged molecules of the immunoglobulin, Fc-area which is the activation of complement.The main quality indicators of intravenous immunoglobulins (IG) is low anticomplementary activity (AKA), the absence of aggregates, low dimers and fragments, the higher content of monomers and stability of these indicators during storage.Most good clinical tolerability and low anticomplementary activity are immunoglobulins obtained by enzymatic treatment with pepsin /1/. But cleaved by pepsin immunoglobulin (trade name "Gammavision", Germany) is characterized by a low content of the most physiologically active Monomeric fraction, the absence of the FC part of the neck with the help of other enzymes - trypsin or plasmin /4/ require a long process of splitting within 14-28 days /5/ and due to their optimum action at neutral pH and cannot be completely removed from the drug proteolysis proceeds even at a temperature of 4oC.Currently, all known drugs of intravenous IG prepared by cleavage with pepsin, derived from sediment II at Stake deposition denaturing high concentration of ethanol 25% at neutral pH isoelectric point of the IG, when the immunoglobulin least stable.When receiving intravenous IG from the precipitate II to reduce the AKA to 20 mg of protein requires the actual splitting of the monomer molecules of the IG to fragments (25-80%). At the same time, the implementation of proteolysis IG at low ionic strength (in distilled water) were obtained from the precipitation II without the /6/ and ultrafiltration at a pH of 4.0 is not possible to reduce the AKA to values greater than 5 mg without additional purification stages and is accompanied by the appearance of aggregates up to 2-3% /7/, which is unacceptable.Reducing some researchers concentration of sodium chloride in the process of proteolysis from 0.9% to 0.45% /8/ reduced content of aggregates up to 2.5%. Use for stabilized quite expensive and long-low-tech procedure /9/.Subsequent removal of proteases with aluminum hydroxide at a pH of 4.0 in the physiological solution of sodium chloride /10/, at a pH of 4.0 in the presence of glycine in distilled water /7/, at pH 5.8 to 6.1 /11/, pH 5.5 and 6.5 under 50oC /12/, anionoobmennika at a pH of 6.5 /6/ or pH 7-8 /13/, ultrafiltration at neutral pH against of 0.45% sodium chloride solution /14/ according to the results presented by the authors, is accompanied by the appearance of the units.The final form of the drug may be either liquid or lyophilized. The cooking liquid form of the drug is less time-consuming, but it is unstable performance during storage and transportation. Thus, considered to be the most stable immunoglobulins with a pH of 4.0 in the form of a solution prepared without the use of pepsin was purchased after several months of storage high anticomplementary activity and up to 3% of the aggregated molecules /15,16/.Lyophilization creates conditions that are independent of the conditions of transportation, but these drugs can have long dissolved, and the lyophilization may cause units /17/, increase anticomplementary activity /18/ and the appearance of opalescence.The closest technical receieved obtaining raw sludge fraction III con his lyophilization and subsequent dissolution, the introduction of stabilizers - glycine and glucose, the addition of pepsin at a pH of 3.9 to 4.0, the hydrolysis of an antibody for 18 hours at a temperature of 37oC, subsequent treatment with aluminum hydroxide to remove the enzyme maturation of the product at pH 6,0-6,4 to form volatile impurities and their removal by centrifugation, separation of the target product.The disadvantage of this method is a multi-stage process, the need for freeze-drying of raw sludge immunoglobulin to remove ethanol. The presence of an intermediate stage of drying is not possible to release the final product in dried form, since the repeated drying leads to the formation of aggregates in the target product. Therefore, FS 42-3159-95 there is only liquid form of intravenous immunoglobulin with a shelf life of only one year.A serious disadvantage is the need for long-term maturation of the drug to form a precipitate unstable globulins and their subsequent separation. The formation of unstable globulin is associated with poorly controlled parameters of the technological process, images of the SS="ptx2">The liquid form of the immunoglobulin prepared according to the prototype, less stable, and with repeated shaking of the vials that occurs during transportation, the indicators of the quality of the product deteriorates. In particular, anticomplementary activity increased with 10 mg protein not binding 2 CH50, to 5 mg, appear aggregated forms of the antibody.The challenge which seeks the invention is to improve the quality of the target product, the simplification and reduction of the technological cycle of production of the drug, increasing the shelf life of the target product.The technical result consists in obtaining intravenous immunoglobulin, stable main indicators during the entire period of storage, and the simplification of the manufacturing process.The essence of the method consists in the following: as an initial solution for the preparation of intravenous immunoglobulin use the filtrate III, who concentrated by ultrafiltration at a pH of 3.8 to 4.5, followed by diafiltration against distilled water, the treatment with pepsin and removing the aluminum hydroxide is carried out in the presence of sugars and when the chloride content is neigh NaCL, the resulting preparation for selection later use in liquid or dry form.Alternatively pepsin can be removed by ultrafiltration or dialysis, or anion exchange chromatography, the desired product may have a pH value of 4.0 to 4.5, and a dry form of the drug must contain additional stabilizer - maltose.Unlike the prototype of the claimed method differs from the known fact that the quality of raw materials used, the filtrate III, applied ultrafiltration and diafiltration at pH 3.8 to 4.5 using distilled water, the treatment with pepsin and its removal is carried out in the presence of sugars, the absence of glycine and when the chloride content is less than 0.2%, and only after that enter glycine, the end product can be used both in liquid and dry form.The set of distinctive features of the proposed method allows to obtain the following advantages.The use of ultra - and diafiltration of centrifugate III at Stake for the initial preparation of the solution instead of the alcohol precipitation, receiving raw sludge immunoglobulin and its freeze-drying allows to obtain the target product is stable for more than the temperature of the 37oC for 14 days, which corresponds to the storage immunoglobulin for 1 year at a temperature of 2-6oC, the samples immunoglobulin prepared in accordance with the prototype, created a significant number of aggregated molecules and almost 2-fold increase in the content of the fragments. In samples of immunoglobulin prepared by the present method, slightly increased only the number of fragmented molecules.The stage of hydrolysis of immunoglobulin with pepsin and its subsequent removal in the absence of glycine and chloride content less than 0.2% helps prevent the formation of soluble forms of aluminium hydroxide and thereby reduce the salt content of aluminum in the target product. Application as an option for removal of pepsin method of ultrafiltration, or dialysis, or anion-exchange chromatography allows you to completely excluded from the process using aluminum hydroxide.At this process step is the removal of pepsin, which is adsorbed with aluminum hydroxide and insoluble form of aluminium hydroxide removes calcium more efficiently. By ultrafiltration or dialysis pepsin Takala requirements of the European Pharmacopoeia for drugs intravenous - not more than 200 μg/L. In commercial samples of immunoglobulin (prototype) the number of aluminum ions was 1492,5 µg/l, which apparently promotes the formation of aggregates in drug test "accelerated aging" (PL. 1).Residual proteolytic activity (PA) in terms of 1 µg of tyrosine, on which is based the calibration graph, in samples of immunoglobulin prepared according to the prototype, was not determined, whereas the PA samples immunoglobulin prepared according to the prototype, ranged from 2 to 8 ág/L. Therefore, by the end of shelf life in liquid form of the drug on the prototype significantly increases the content of the fragments.The combination of the application of the techniques of ultra - and diafiltration of centrifugate III for the preparation of the starting solution, the holding stage hydrolysis in the presence of sugars in the chloride content of less than 0.2%, the introduction of glycine after hydrolysis step and the use of additional stabilizer (maltose) allows you to: reduce the content fragments; to prevent the formation of aggregated forms of immunoglobulin during freeze-drying of the target product; to prevent the formation of unstable impurities and aggregates in immunodeficiency, the second product and to reduce the duration of the process.Thus, the transparency of the product prior to drying is 0,0080 0,00026, after freeze-drying practically does not change and is 0,0083 0,00031.The combination of these techniques provides the stability of the main indicators of the quality of the drug (anticomplementary activity and lack of units) for 2 years. The stability of the main indicators of immunoglobulin provided Pharmacopoeial article, are presented in table. 3.Intravenous immunoglobulin was obtained as follows.The filtrate "B" (corresponding to fraction III method Kona), is a purified immunoglobulin solution with a pH of 5.1 and 5.4, the ethanol content of 17-20% and a protein content of 0.35 to 0.4% is collected in a container (reactor) and corrects the pH to 4.0 and 4.3, and then subjected to concentration by ultrafiltration installation with membranes with a limit of cut-off molecular weight of 50 to 100 thousand daltons (mol. the mass of the molecules of the immunoglobulin 160 thousand days). After reduction of the volume of solution in 10-12 times are shaded from ethanol by continuous supply of distilled water to a volume of 3-5 times more than the volume of the solution of the immunoglobulin. Then concentrate the solution to a protein content of 8-9% and adjusting the pH value dt hydrolysis for 18 hours at a temperature of 37oC. removal of pepsin to the solution of the immunoglobulin type aluminium hydroxide, mix and remove complex pepsin - aluminium hydroxide by centrifugation. After that enter stabilizers, set in the target product a pH value of 6.5-7.5, the required amount of sodium chloride, adjusting the protein concentration to 4.5-5.5% and spend sterilizing filtration. The target product is poured into vials. If necessary, the product can be dried.In the second variant of the method of destruction of pepsin may be held or ultrafiltration, or dialysis at pH 3.8 to 4.5, or anion-exchange chromatography at a pH of 4.0 to 5.7. In the preparation of the dry form of the drug is injected additional stabilizer - maltose at a concentration of 1-5%, the target product can have a pH value of 4.0 to 4.5.Example 1 (option 1).The filtrate "B" in the amount of 200 l with a pH of 5.3 is pumped into the reactor and using 1 N HCL solution corrects the pH to 4.1 and subjected to concentration by ultrafiltration installation with membranes UPM-100 with filter area of 6 square meters for 3 hours. After reduction of the solution volume up to 20 l reactor start continuously feeding 95-100 l with distilled water to remove atenolol - glucose at a concentration of 2%, set the pH value of 3.9 and enter pepsin. The chloride content is 0.04%. The solution is filtered through a sterilizing filter and carry out hydrolysis for 18 h at 37oC. the Pepsin is removed by addition of aluminum hydroxide and removing the complex aluminum hydroxide - pepsin by centrifugation. After that enter the stabilizer - glycine in a concentration of 1%, set the content of protein in the solution is 5 to 0.5%, pH 7.0 0.5%, and the chloride content of 0.85%, immunoglobulin subjected to sterilizing filtration and poured into bottles.Example 2 (option 2).The filtrate "B" in the amount of 100 l with a pH of 5.4 is pumped into the reactor, corrects the pH to 4.2 and subjected to concentration by ultrafiltration plant with filtration area of 4 square meters for 2 hours. After reduction of the volume of the solution up to 10 l in the reactor serves 45-50 liters of distilled water and concentrated to a protein content of 8.5%, receiving 2.5 l of immunoglobulin. The chloride content is 0.15%. Enter stabilizer - maltose at a concentration of 2%, set the pH value of 3.9 and enter pepsin. The solution is filtered through a sterilizing filter and carry out hydrolysis for 18 h at 37oC. the Pepsin is removed by re-diafiltration of 3.9. After that enter stabilizers - glucose at a concentration of 2% glycine in a concentration of 1%, maltose at a concentration of 2%, set the content of protein in the solution is 5 to 0.5%, pH of 4.25 0.25 per cent, the immunoglobulin is subjected to sterilizing filtration, poured into vials and subjected to freeze-drying.Example 3. Concentration of the filtrate "B", the exemption from ethanol and hydrolysis process immunoglobulin performed as in example 1-2. Residual pepsin, the products of fission and lipoprotein removed by addition of anion-exchanger, such as DEAE-sepharose in the amount of 10 g per 1 l of a solution of immunoglobulin when the pH value of 4.3. After stirring solution of immunoglobulin with the sorbent for 30 min aminoalkenes removed by filtration. After that enter stabilizers - glucose at a concentration of 2% glycine in a concentration of 1%, maltose at a concentration of 5%, set the content of protein in the solution is 5 to 0.5%, pH of 4.25 0.25 per cent, the immunoglobulin is subjected to sterilizing filtration, poured into vials and subjected to freeze-drying.Example 4. Concentration of the filtrate "B", the exemption from ethanol and hydrolysis process immunoglobulin performed as in example 1-2. For Dalenergo and placed in solution with distilled water at a pH of 4.0. Distilled water is changed 2 to 3 times. After dialysis enter stabilizers - glucose at a concentration of 2% glycine in a concentration of 1%, set the content of protein in the solution is 5 to 0.5%, pH 7.5 with 0.5%, NaCl 0,9%, immunoglobulin subjected to sterilizing filtration and poured into bottles.Literature
1) Romer J., Spath P. J., Skvaril F., Nydegger, U. E. Characterization of various Immunoglobulin preparations for intravenous application. ii. Complement activation and binding to staphylococcus protein A. Vox Sang., 1982, 42, 76.2) Schultze, H. E., G. Schwick Uber neue Moglichkelten intravenoser Gammaglobulin-Application. Dt. med. Wschr., 1962, 87: 1643-1650.3) High quality lgG produced with q Sepharose Fast Flow. Downstream 21. Plasma fractionation by chromatography. Pharmacia Biotech, 18-1115-62, p. 6.4) German Patent 2752694, C0797/00. Plasminogen immunoglobulins. Publ. 21.01.81.5) Patent Of England N 1469908, A 61 K 39/395. Obtaining enzymes to remove anticomplementary of immunoglobulins. Publ. 09.02.73.6) Patent of Switzerland CH 684164 A5, A 61 K 39/395. Intravenous immunoglobulin used solution. Publ. 10.01.92.7) Anastasiav centuries the Development of technology for next-generation antibodies for the treatment of infectious and autoimmune diseases. The dissertation on competition of a scientific degree of the doctor of biological Sciences. Moscow 1997, 1-49.10) Anastasiav Centuries, Kiseleva, I. A., Novikova L. P., Turaeva, A. // Hematol. and Transfusiology. - 1985. - 10. - S. 46-48.11) European patent EP 0085747, A 61 K 39/395. Intravenous human immunoglobulin and a method thereof. Publ. 184.108.40.206) Grandgeorge M., F. Pelloquin Inactivation of the human immunodeficiency viruses (HIF-1 and HIF-2) during the manufacturing of placental albumin and gammaglobulins. /Transfusion 1989, 29,7,629-634/).14) French Patent N 2582515, A 61 K 39/395. The preparation of intravenous immunoglobulin. Publ. 18. 03. 85.15) J. Ring, Duswald K. H., Seifert J., Brendel W. Immunologische Properties, Aggregatgehalt und Halbwertszeit verschiedener 1. v. Human-Gamma-Globulinpraparate. Langenbecks Archiv fur Chlrurgle, 1976 supplement. Chirurgisches Forum 76 für experimentelle und klinische Forschung. 93. Kongres der Deutschen Gesellschaft fur Chirurgie. Munchen 1976, 63-66)
16) Barandun S., Isliker H. Development of immunoglobulin preparations for intravenous use. Vox Sang., 1986, 51, 159.17) Hansson U. B. Aggregation of human immunoglobulin Gupon freezing. Acta Chem. Scand. 1968, 22, 483-9),
18) R. Audran, M. Steinbuch Etude des conditions dapparition et de preventlonde lactivite anticomplementaire des globulines G. Prot. Biol. Fluids, Elsevier, 1967, vol. 15, p. 479.19) Patent RU 2068695, A 61 K 35/16. - Publ. 10.11.96.20) guidelines for the application of physico-chemical, chemical and immunochemical methods for the control of drugs immunoglobulin. The USSR Ministry of health, 1982, S. 34-37.1. The method of producing immunoglobulin for intravenous administration, comprising preparing a starting solution stabilizers, processing pepsin at a pH of 3.9 to 4.0, then remove pepsin aluminum hydroxide and isolation of the target product, characterized in that for obtaining an initial solution using the filtrate W, which is concentrated by ultrafiltration at a pH of 3.8 to 4.5, followed by diafiltration against distilled water, the treatment with pepsin and removing the aluminum hydroxide is carried out in the presence of sugars and chloride content less than 0.2%, then enter glycine, establish a pH value of 4.0 - 7.5, the content of 4.5 - 5.5% and physiological NaCL, the resulting preparation for selection later use in liquid or dry form.2. The method of producing immunoglobulin for intravenous administration, comprising preparing a starting solution, the introduction of stabilizers, processing pepsin at a pH of 3.9 to 4.0, the subsequent removal of pepsin and isolation of the target product, characterized in that for obtaining an initial solution using the filtrate W, which is concentrated by ultrafiltration at a pH of 3.8 to 4.5, followed by diafiltration against distilled water, the treatment with pepsin prom, or by anion-exchange chromatography, and then enter glycine, establish a pH value of 4.0 - 7.5, the protein content of 4,5 - 5,5% received the drug for choice later use in liquid or dry form.3. The method according to PP.1 and 2, characterized in that to obtain the dry form of the drug use more stabilizer - maltose at a concentration of 1 - 5%.4. The method according to p. 2, characterized in that the anion-exchange chromatography to remove pepsin and ballast impurities after proteolysis is carried out at a pH value of 4.5 to 5.7.5. The method according to p. 2, characterized in that the ultrafiltration or dialysis to remove pepsin and ballast impurities after proteolysis is carried out at a pH value of 3.8 to 4.5.6. The method according to PP.1 to 5, characterized in that the target product is obtained with a pH of 4.0 to 4.5.
FIELD: genetic engineering, immunology, medicine.
SUBSTANCE: invention relates to new antibodies directed against antigenic complex CD3 and can be used in therapeutic aims. Antibody IgG elicits the affinity binding with respect to antigenic complex CD3 wherein heavy chain comprises skeleton of the human variable region in common with at least one CD3 taken among amino acid sequences SEQ ID NO 2, 4 and 6 and their corresponding conservatively modified variants. Light chain comprises skeleton of the rodent variable region in common with at least one CD3 taken among amino acid sequences SEQ ID NO 8, 10 and 12 and their corresponding conservatively modified variants. Antibody is prepared by culturing procaryotic or eucaryotic cell co-transformed with vector comprising recombinant nucleic acid that encodes antibody light chain and vector comprising recombinant nucleic acid that encodes antibody heavy chain. Antibody is administrated in the patient suffering with malignant tumor or needing in immunosuppression in the effective dose. Invention provides preparing chimeric antibodies against CD3 that are produced by expression systems of procaryotic and eucaryotic cells with the enhanced yield.
EFFECT: improved preparing methods, valuable medicinal properties of antibody.
33 cl, 5 dwg, 1 ex
FIELD: medicine, pharmaceutical industry and technology, pharmacy.
SUBSTANCE: invention relates to a composition eliciting an antiviral effect. The composition comprises hydrophilic conglomerate of immunoglobulins consortium adsorbed with polyethylene glycol 4000-6000, recombinant interferon-α2 and a special additive taken among the following substances: glycine, glucose, maltose, sodium chloride taken in the definite ratio of components. Invention provides elevating solubility of composition eliciting an antiviral effect and enhanced release of biologically active substances to solution.
EFFECT: valuable medicinal properties of composition.
FIELD: medicine, pharmacy.
SUBSTANCE: invention relates to a composition eliciting an antibacterial effect. Composition comprises hydrophilic conglomerate of immunoglobulins consortium adsorbed with polyethylene glycol 4000-6000 and a special additive taken among the following substances: glycine, glucose, maltose, sodium chloride taken in the definite ratio of components. Invention provides sufficient desorption of biologically active substances in resuspending the composition eliciting an antibacterial effect and comprising consortium of immunoglobulins.
EFFECT: valuable medicinal properties of composition.
SUBSTANCE: the innovation deals with new immunogenic conjugates of beta-propionamide-bound polysaccharide and N-propionamide-bound oligosaccharide with protein, and the method to obtain these conjugates has been suggested, as well. Conjugates should be applied to obtain vaccines against infectious diseases and cancer that enables to broaden the number of preparations applied in treating the above-mentioned diseases.
EFFECT: higher efficiency.
1 dwg, 2 ex, 8 tbl
FIELD: microbiology and immunology, in particular immunodiagnosis.
SUBSTANCE: atypical strain of melioidose Burkholderia pseudomallei-111-6-1 with altered phenotype defected with respect to synthesis of 8 antigen and acting as immunosuppressor is used as antigen for animal immunization. Immune serum is obtained after 2 immunization cycles of animal-producer with titer in gel immunodiffusion reaction not less than 1:128.
EFFECT: immune serum with increased specific activity.
2 tbl, 2 ex
FIELD: medicine and immunology, in particular treatment and prevention immunodeficiency conditions and diseases associated with bacterial or viral aggression.
SUBSTANCE: claimed method includes administration to a patient immunoglobulin drug (e.g., pharmaceutical composition containing 6-12 % of specific heterologous secreted immunoglobulin A, isolated from milk or foremilk of immunized ungulates). Administration is performed parenterally wherein single dose is at least 10 IU/kg of patient weight for treatment or at least 5 IU/kg for prophylaxis; or perorally in dose of 0.2-0.5 g and/or topically one-two times per day for 1-5 days. Method of present invention makes it possible to decrease dose of administrating immunoglobulin due to prolonged retention of its high titers in body fluids.
EFFECT: enlarged range of application and assortment of immunoglobulin drugs.
4 cl, 5 ex
SUBSTANCE: the present innovation deals with cryoprotective ointment containing recombinant interferon-α2. The suggested cryoprotective ointment contains recombinant interferon-α2, glycerol, polyethylene glycol 300-6000, polyglucin, buffered 0.02%-Trilon B solution at pH of 5.5-7.0 and ointment foundation at a certain content of components per 1.0 g ointment. Additionally, cryoprotective ointment could contain glycine 3,7-bis(dimethylamino)phenothiazonium chloride, dry immunoglobulin preparation or dry immunoglobulin preparation for enteral application. Ointment foundation of cryoprotective ointment could contain water-free lanolin, Vaseline and Vaseline oil, at the following ratio of components: 2.5;3.5:1 - 6.5:0.5:1. The innovation provides maximal safety of recombinant interferon-α2 activity in cryoprotective ointment at multiple alteration of positive and negative environmental temperature and at keeping cryoprotective ointment under these conditions.
EFFECT: higher efficiency of application.
8 cl, 8 ex
FIELD: medicine, pharmaceutics, pharmacology.
SUBSTANCE: one should apply mammalian anti-HBP-antibodies. The ways are being suggested to identify monoclonal antibody bound, at least, with one epitope upon native HBP (heparin-binding protein) and methods to detect whether a mammal produces HBR being bound with a monoclonal antibody and, also, the kits for the above-mentioned purpose. The present innovation provides the opportunity to apply the mentioned antibodies in preventing and treating disorders associated with bradykinin releasing.
EFFECT: higher efficiency of application.
25 cl, 11 dwg, 3 ex, 1 tbl
FIELD: veterinary science.
SUBSTANCE: animals should be introduced with antihistamine serum (AHS) subcutaneously at the dosage of 4.0-5.0 ml in combination with myxoferon at the quantity of 60-75 dosages and vitamin C at the dosage of 1.0-1.5 ml/animal, once daily, thrice at interval of 5-7 d. Application of AHS in combination with myxoferon and ascorbic acid provides active stimulation of immunological reactivity, increases total body resistance I animals and causes no toxic effects and allergic reactions.
EFFECT: higher efficiency of correction.
FIELD: immunology, biotechnology, medicine.
SUBSTANCE: invention relates to antiidiotypical monoclonal antibody or fragment thereof for BSW17 antibody effecting on LgE Cε3-region bonding to high affinity LgE receptor. Amino acid sequence is as described in specification. antiidiotypical antibody is useful as pharmaceutical composition ingredient for LgE-mediated disease treatment. Invention make in possible to prevent allergic disorders and inflammations due to inhibiting interaction between LgE Cε3-region with high affinity receptor by claimed antibody.
EFFECT: new agent for allergic and inflammation disorder treatment.
7 cl, 32 dwg, 5 tbl, 10 ex