WO2001030373A1 - Composition polypeptidique - Google Patents
Composition polypeptidique Download PDFInfo
- Publication number
- WO2001030373A1 WO2001030373A1 PCT/RU2000/000427 RU0000427W WO0130373A1 WO 2001030373 A1 WO2001030373 A1 WO 2001030373A1 RU 0000427 W RU0000427 W RU 0000427W WO 0130373 A1 WO0130373 A1 WO 0130373A1
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- Prior art keywords
- mass
- polypeptide
- insulin
- composition
- concentration
- Prior art date
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- 229920001184 polypeptide Polymers 0.000 title claims abstract description 15
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 14
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 14
- 239000000203 mixture Substances 0.000 title abstract description 39
- 239000000945 filler Substances 0.000 claims abstract description 4
- 150000007524 organic acids Chemical class 0.000 claims abstract description 4
- 238000000034 method Methods 0.000 claims description 11
- 150000001875 compounds Chemical class 0.000 claims description 5
- 238000010521 absorption reaction Methods 0.000 claims description 4
- 230000002401 inhibitory effect Effects 0.000 claims description 3
- 239000003814 drug Substances 0.000 abstract description 12
- 239000003112 inhibitor Substances 0.000 abstract description 9
- 108010064983 Ovomucin Proteins 0.000 abstract description 4
- 238000002360 preparation method Methods 0.000 abstract description 3
- 230000002797 proteolythic effect Effects 0.000 abstract 2
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 abstract 1
- 108010000912 Egg Proteins Proteins 0.000 abstract 1
- 102000002322 Egg Proteins Human genes 0.000 abstract 1
- 101710126321 Pancreatic trypsin inhibitor Proteins 0.000 abstract 1
- 241000862632 Soja Species 0.000 abstract 1
- 229940122618 Trypsin inhibitor Drugs 0.000 abstract 1
- 101710162629 Trypsin inhibitor Proteins 0.000 abstract 1
- ZPNFWUPYTFPOJU-MPSLMFKFSA-N aprotinin Chemical compound CC[C@H](C)[C@@H]1NC(=O)[C@@H](CCCNC(N)=N)NC(=O)[C@@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]2CSSC[C@H]3NC(=O)CNC(=O)CNC(=O)[C@H](Cc4ccc(O)cc4)NC(=O)[C@H](NC(=O)[C@H](Cc4ccccc4)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](CSSC[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](Cc4ccccc4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC3=O)C(=O)N[C@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](CSSC[C@@H](NC(=O)[C@H](Cc3ccccc3)NC(=O)[C@@H](CC(O)=O)NC(=O)[C@H]3CCCN3C(=O)[C@H](N)CCCNC(N)=N)C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N3CCC[C@@H]3C(=O)N3CCC[C@H]3C(=O)N[C@H](Cc3ccc(O)cc3)C(=O)N[C@H]([C@H](C)O)C(=O)NCC(=O)N3CCC[C@H]3C(=O)N2)C(=O)NCC(=O)NCC(=O)N[C@H](C)C(O)=O)NC(=O)[C@@H](CC(C)C)NC(=O)CNC(=O)[C@@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](Cc2ccc(O)cc2)NC(=O)[C@H](Cc2ccccc2)NC(=O)[C@@H](Cc2ccc(O)cc2)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](NC1=O)[C@H](C)CC)[C@@H](C)O)C(C)C ZPNFWUPYTFPOJU-MPSLMFKFSA-N 0.000 abstract 1
- 235000014103 egg white Nutrition 0.000 abstract 1
- 210000000969 egg white Anatomy 0.000 abstract 1
- 239000000463 material Substances 0.000 abstract 1
- 210000004400 mucous membrane Anatomy 0.000 abstract 1
- 230000035515 penetration Effects 0.000 abstract 1
- 239000002753 trypsin inhibitor Substances 0.000 abstract 1
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 70
- 102000004877 Insulin Human genes 0.000 description 35
- 108090001061 Insulin Proteins 0.000 description 35
- 229940125396 insulin Drugs 0.000 description 35
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 27
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 16
- 239000008103 glucose Substances 0.000 description 16
- 102000004169 proteins and genes Human genes 0.000 description 12
- 108090000623 proteins and genes Proteins 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 229940079593 drug Drugs 0.000 description 8
- 235000013601 eggs Nutrition 0.000 description 8
- 230000007423 decrease Effects 0.000 description 7
- 210000002784 stomach Anatomy 0.000 description 7
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 5
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 239000008101 lactose Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 210000002700 urine Anatomy 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 235000010469 Glycine max Nutrition 0.000 description 4
- 230000002378 acidificating effect Effects 0.000 description 4
- 230000037396 body weight Effects 0.000 description 4
- 210000000936 intestine Anatomy 0.000 description 4
- 241000272525 Anas platyrhynchos Species 0.000 description 3
- 102000018997 Growth Hormone Human genes 0.000 description 3
- 108010051696 Growth Hormone Proteins 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 239000000122 growth hormone Substances 0.000 description 3
- 108010000437 Deamino Arginine Vasopressin Proteins 0.000 description 2
- 244000068988 Glycine max Species 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 229960004281 desmopressin Drugs 0.000 description 2
- NFLWUMRGJYTJIN-NXBWRCJVSA-N desmopressin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSCCC(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(N)=O)=O)CCC(=O)N)C1=CC=CC=C1 NFLWUMRGJYTJIN-NXBWRCJVSA-N 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000029142 excretion Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 239000003262 industrial enzyme Substances 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 230000037081 physical activity Effects 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 229920002717 polyvinylpyridine Polymers 0.000 description 2
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 2
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 2
- WSWCOQWTEOXDQX-MQQKCMAXSA-M (E,E)-sorbate Chemical compound C\C=C\C=C\C([O-])=O WSWCOQWTEOXDQX-MQQKCMAXSA-M 0.000 description 1
- 241000272517 Anseriformes Species 0.000 description 1
- 241000167854 Bourreria succulenta Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 229920000168 Microcrystalline cellulose Polymers 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 206010039509 Scab Diseases 0.000 description 1
- 241000555745 Sciuridae Species 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 210000000941 bile Anatomy 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000019693 cherries Nutrition 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 239000003651 drinking water Substances 0.000 description 1
- 235000020188 drinking water Nutrition 0.000 description 1
- 208000000718 duodenal ulcer Diseases 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- -1 for example Substances 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 210000001156 gastric mucosa Anatomy 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 210000002429 large intestine Anatomy 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 235000019813 microcrystalline cellulose Nutrition 0.000 description 1
- 239000008108 microcrystalline cellulose Substances 0.000 description 1
- 229940016286 microcrystalline cellulose Drugs 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229940124531 pharmaceutical excipient Drugs 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229940127557 pharmaceutical product Drugs 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920006316 polyvinylpyrrolidine Polymers 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 229960004889 salicylic acid Drugs 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229940075554 sorbate Drugs 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 229940124788 therapeutic inhibitor Drugs 0.000 description 1
- 210000001635 urinary tract Anatomy 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/28—Insulins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/27—Growth hormone [GH], i.e. somatotropin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/56—Protease inhibitors from plants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
Definitions
- the invention is subject to the field of medicine, biochemistry and biotechnology, and it is the personalized medicine used in medicine for the treatment of by-drug
- the gastric fluid in the process of digestion passes into the duodenal ulcer, where it mixes with bile and the gastric gland.
- the pharmaceutical products contained in the pan-therapeutic system trypsin and other hydrolyze the reaction with amine-derived substances.
- the normal conditions of the protein are almost completely extended to Their constituent amino acids, which are then rapidly absorbed in the intestine. It is possible that some hydraulic processes (for example, in the case of illnesses) are fully completed at an intestinal rate. [. The biology of man. Russia, intersect ⁇ , 1993. p. 284-297].
- a known polypeptide compound consisting of (% wt.) 0.001 - 0.5 polypeptides, as a rule uses insulin, 1, 0-30.0 polimerpa. modified inhibition of industrial enzymes, and 70-98 water [Patent of the Russian Federation Ya ⁇ ”2066551. ⁇ I ⁇ 61 ⁇ 38/28, BI . ⁇ . 29, 1996].
- First use of this combination reduces the glucose level at 53% of the time when the initial insulin dose is 10 units / kg.
- ⁇ es ⁇ the purpose ⁇ bes ⁇ echeniya v ⁇ zm ⁇ zhn ⁇ s ⁇ i ⁇ e ⁇ aln ⁇ g ⁇ ⁇ imeneniya ⁇ m ⁇ zitsii her ⁇ yvayu ⁇ zhelud ⁇ chn ⁇ - ⁇ ezis ⁇ en ⁇ n ⁇ y ⁇ b ⁇ l ⁇ ch ⁇ y, ⁇ aya not ⁇ as ⁇ v ⁇ yae ⁇ sya in zhelud ⁇ e, n ⁇ ⁇ as ⁇ v ⁇ yae ⁇ sya in ⁇ n ⁇ m ⁇ ishechni ⁇ e with vysv ⁇ b ⁇ zhdeniem ⁇ m ⁇ zitsii and s ⁇ de ⁇ zhascheg ⁇ sya it ⁇ li ⁇ e ⁇ ida.
- the disadvantage of this combination is the complexity of its use (inability to perform gastric-impaired treatment) and a low incidence of infection.
- the maximum decrease in the concentration of glucose at home after the introduction of a com- pensation is 47% of the original level.
- the com- pact contains insulin, and in the capacity of inhibitors of enzymes, it inhibits the metabolism of soy.
- the company uses it by distributing it in a physiological process (0.9% recovery of sodium chloride) to achieve a percentage increase of 0.0%. (5 mg per 10 ml) with the subsequent introduction of 1 ml of the solution is not immediately available in the intestine of the livestock.
- the indicated product may also contain a protective polimer, antioxidant, inhibitory enzyme and non-organic salt.
- the disadvantage of this device is the inability to use it inappropriately for the administration of a drug.
- the composition of the product does not ensure the protection of the constituent in it from the harmful effect of the acidic environment of the stomach. Therefore, before the oral administration of the product, the patient is introduced to the body for complete neutralization of the acid of the stomach. And although the physical activity is known to be relatively high (for example, the rapid introduction of 10 units of insulin into the body with diabetes has a high incidence of fatal illness)
- the company uses it in its use in water or in a physiological process to achieve a concentration of the substance
- the combination may additionally contain the known compounds, which accelerate the absorption process, by a factor of 10 to 5, more than.
- Example 1 The composition contains 15 mg of insulin (3.0% of the mass), 0.1 mg (0.02
- a pan-therapeutic inhibitor of trypsin 470 mg (94% of the mass) of citric acid and 14.9 mg (2.98% of the mass) of lactose.
- the molecular mass of insulin is 6500.
- the composition is dissolved in 100 ml of physiological solution of insulin concentration equal to 0.015% of the mass) and 6.7 ml
- the resulting solution (25 units of insulin) transfers the drug to the patient. Samples are at risk of testing and after 30, 60, 90, 120 and 150 minutes after the introduction of the drug. The results are presented in table 1.
- the composition contains 10 mg of insulin (2.0% of the mass), 0.1 mg (0.02% of the mass) of soybean inhibitor of trypsin, 1.0 mg (0.2% of the mass) of citric acid and 488.9 mg (97, 78% of the mass) of carboxymethyl cellulose.
- the composition is dissolved in 100 ml of a physiological solution (insulin concentration is equal to 0.01% of the mass) and 10 ml of the obtained solution (25 units of insulin) is converted. The results are presented in table 1.
- the composition contains 10.98 mg of insulin (42.23% of the mass), 0.01 mg (0.04% of the mass) of ovomucoid from the protein of ducks, 15 mg (57.69% of the mass) of citric acid and 0.01 mg (0 , 04% of the mass) of polyvinylpyrrolide.
- composition is distributed in 100 ml of physiological solution (concentration of insulin is equal to 0.011% of the mass) and 9.1 ml of the obtained solution (25 units of insulin) is converted.
- concentration of insulin is equal to 0.011% of the mass
- 9.1 ml of the obtained solution 25 units of insulin
- composition contains 14.5 mg of insulin (15.3% of the mass), 0.2 mg
- the composition contains 20.5 mg of insulin (97% of the mass), 0.17 mg (0.8% of the mass) of ovomucoid from the protein of duck eggs, 0.4 mg (2.0% of the mass) of citric acid and 0.04 mg ( 0.2% of the mass) of the lactose.
- the composition is distributed in 100 ml of physiological solution (concentration of insulin is equal to 0.0205% of the mass) and 4.9 ml of the resulting solution (25 units of insulin) are converted. The results are presented in table 1.
- Table 1 The effect of the administration of a live substance containing 1 mg of insulin in the composition of the claimed composition to the concentration of glucose in the body.
- Whites are placed in the cage-pens for the removal of urine and within 120 minutes, the excretion of urine in the urinary tract is registered. Without the introduction of an internal load, crusts excrete 0.4 ⁇ 0.04 ml of urine per 100 g of body weight in 120 minutes. 15 and at the end of the meal, 5 ml of water per 100 g of body weight are injected into the stomach with a probe. In 120 minutes, these flavors excrete 4.42 ⁇ 0.19 ml of urine per 100 g of body weight.
- composition contains 0.004 mg (95% of the mass) of desmopressin - polypeptide (molecular weight of 1069), which decreases the excretion of milk, 0.000042 mg (1% of the mass) of carbohydrate protein of eggs, 0.000042 mg (1%) 00013 (3% of the mass) of sugar.
- the mixture is dissolved in 100 ml of water (the concentration of desmopressin is equal to 0.000004% of the mass) and this solution is injected into the stomach of 11 ml and the mass is 5 ml per 100 g. 120 For 120 minutes, the separation of blood from the body is 1.1 1 ⁇ 0.41 ml of urine per 100 g of body weight, that is, it will be reduced 4 times after the introduction of the drug.
- Example 12 The composition contains 0.04 mg (93% of the mass) of desmessess,
- the concentration is increased in 100 ml of water (concentration
- the dispersion is equal to 0.00004%> mass) and the tests are carried out at 9th and at 7th level. For 120 minutes, the discharge at the moment is completely suppressed.
- Example 13 The composition contains 10 mg of glucose (80%> mass), 1.25 mg of inhibitor of trypsin from soya (10% of the mass), 0.2 mg of citric acid (1.6% of the mass) and 1.05 mg of polyvinylpyridine , 4% of the mass).
- the molecular weight of the glucone is equal to 3500.
- the composition is dissolved in 100 ml of water (the concentration of glucogen is equal to 0.01% of the mass) and 10 ml of the solution is discharged.
- the concentration of glucose in the blood is measured after 5, 10, 20, 30 and 60 minutes. The results are shown in table 2.
- the composition contains 100 mg of glucagon (98% by weight), 1, 02 mg of inhibitor of trypsin from soy (1% of the mass), 0.51 mg of citric acid (0.5%> mass) and 0.51 mg of polyvinylpyrrolide (0.5%> )
- the solution is dissolved in 100 ml of water (concentration of glucone is equal to 0.1% of the mass) and 1 ml of solution is added to the solution.
- concentration of glucone is equal to 0.1% of the mass
- 1 ml of solution is added to the solution. The results are shown in table 2.
- the composition contains 15.0 mg (80% of the mass) of the growth hormone (protein with a molecular weight of 21,000), 1.58 mg (8.4%> of the mass) of ovomucoid from the protein of the utensils of eggs, 1.3 mg (6.9% of the mass) Acidic Acid and 0.88 mg (4.7% of the mass) of polyvinylpyrrolidine.
- the composition is distributed in 100 ml of a physiological solution (concentration of the group is equal to 0.015 mass) and 6.7 ml of an increased volume (1 mg of the unit). The results are presented in table 3.
- Example 16 The composition contains 15.0 mg (80%> mass) of the growth medium, 1.58 mg (8.4% of the mass) of the pancreatic acid inhibitor, 0.88 mg (4.7 mass) of citric acid and 1.3 mg (6.9%> mass) of lactose.
- the composition is dissolved in 100 ml of a physiological solution (concentration of the group is equal to 0.015%> of the mass) and 6.7 ml of the obtained product is in bulk (1 mg) The results are presented in table 3.
- the composition contains 100 mg (98% of the mass) of the growth hormone, 0.51 mg (0.5%> of the mass) of utukuida from the protein of the utensils of eggs, 0.51 mg (0.5% of the mass) of the acid and 1.0 mg (1 mg) , 0%> mass) of polyvinylpyrrolide.
- the composition is dissolved in 100 ml of a physiological solution (concentration of the growth group is equal to 0.1%> mass) and 1.0 ml of the obtained product (1 mg of the group)
- Table 3 Dependence of the growth rate of the hormone in the area at the time of administration after the administration of a 1 mg growth hormone.
- the preparation for example, 1, additionally contains 150 mg of sodium lauryl sulfate.
- the results of the test of this combination are given in table 4.
- EXAMPLE 19 The preparation for example 1 additionally contains 750 mg of sodium lauryl sulfate. The test results of this arrangement are shown in Table 4. 14
- the claimed invention ensures that there is no need for mass treatment of masses of up to 1000 to 21000 for industrial use.
- polypeptides are located in a native state, which ensures their inherent physical activity.
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Zoology (AREA)
- Endocrinology (AREA)
- Botany (AREA)
- Diabetes (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AU13162/01A AU1316201A (en) | 1999-10-28 | 2000-10-27 | Polypeptide composition |
IL14935500A IL149355A0 (en) | 1999-10-28 | 2000-10-27 | Polypeptide corporation |
DE10085144T DE10085144T1 (de) | 1999-10-28 | 2000-10-27 | Polypeptidkomposition |
DK200200624A DK200200624A (da) | 1999-10-28 | 2002-04-25 | Polypeptid-præparat |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
RU99122655 | 1999-10-28 | ||
RU99122655A RU2171687C2 (ru) | 1999-10-28 | Полипептидная композиция |
Publications (2)
Publication Number | Publication Date |
---|---|
WO2001030373A1 true WO2001030373A1 (fr) | 2001-05-03 |
WO2001030373A8 WO2001030373A8 (fr) | 2002-02-07 |
Family
ID=20226315
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/RU2000/000427 WO2001030373A1 (fr) | 1999-10-28 | 2000-10-27 | Composition polypeptidique |
Country Status (6)
Country | Link |
---|---|
AU (1) | AU1316201A (de) |
DE (1) | DE10085144T1 (de) |
DK (1) | DK200200624A (de) |
IL (1) | IL149355A0 (de) |
WO (1) | WO2001030373A1 (de) |
YU (1) | YU31902A (de) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2020506882A (ja) * | 2017-01-27 | 2020-03-05 | マイクロファーム・リミテッドMicropharm Limited | 炎症性障害の治療療法 |
Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU94010369A (ru) * | 1994-03-23 | 1996-08-10 | Институт нефтехимического синтеза им. А.В.Топчиева РАН | Способ получения производных инсулина |
WO1996036352A1 (en) * | 1995-05-16 | 1996-11-21 | Pankaj Modi | Liquid formulations for proteinic pharmaceuticals comprising at least 2 absorption enhancers |
WO1998011912A1 (en) * | 1996-09-20 | 1998-03-26 | Neurobiological Technologies, Inc. | Pharmaceutical formulations of corticotropin releasing factor having improved stability in liquid form |
RU2126264C1 (ru) * | 1993-04-07 | 1999-02-20 | Скиос Инк. | Фармацевтическая композиция |
RU2136306C1 (ru) * | 1994-05-04 | 1999-09-10 | Санофи | Стабилизированная протеинсодержащая лиофилизированная композиция |
-
2000
- 2000-10-27 IL IL14935500A patent/IL149355A0/xx unknown
- 2000-10-27 DE DE10085144T patent/DE10085144T1/de not_active Withdrawn
- 2000-10-27 YU YU31902A patent/YU31902A/sh unknown
- 2000-10-27 AU AU13162/01A patent/AU1316201A/en not_active Abandoned
- 2000-10-27 WO PCT/RU2000/000427 patent/WO2001030373A1/ru active Application Filing
-
2002
- 2002-04-25 DK DK200200624A patent/DK200200624A/da not_active Application Discontinuation
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU2126264C1 (ru) * | 1993-04-07 | 1999-02-20 | Скиос Инк. | Фармацевтическая композиция |
RU94010369A (ru) * | 1994-03-23 | 1996-08-10 | Институт нефтехимического синтеза им. А.В.Топчиева РАН | Способ получения производных инсулина |
RU2136306C1 (ru) * | 1994-05-04 | 1999-09-10 | Санофи | Стабилизированная протеинсодержащая лиофилизированная композиция |
WO1996036352A1 (en) * | 1995-05-16 | 1996-11-21 | Pankaj Modi | Liquid formulations for proteinic pharmaceuticals comprising at least 2 absorption enhancers |
WO1998011912A1 (en) * | 1996-09-20 | 1998-03-26 | Neurobiological Technologies, Inc. | Pharmaceutical formulations of corticotropin releasing factor having improved stability in liquid form |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2020506882A (ja) * | 2017-01-27 | 2020-03-05 | マイクロファーム・リミテッドMicropharm Limited | 炎症性障害の治療療法 |
US11098114B2 (en) | 2017-01-27 | 2021-08-24 | Micropharm Limited | Ovine derived human TNFα polyclonal antibody composition for oral administration |
Also Published As
Publication number | Publication date |
---|---|
AU1316201A (en) | 2001-05-08 |
WO2001030373A8 (fr) | 2002-02-07 |
IL149355A0 (en) | 2002-11-10 |
YU31902A (sh) | 2004-12-31 |
DK200200624A (da) | 2002-06-21 |
DE10085144T1 (de) | 2003-04-24 |
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