JP6857613B2 - タンパク質の安定化 - Google Patents
タンパク質の安定化 Download PDFInfo
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- JP6857613B2 JP6857613B2 JP2017551685A JP2017551685A JP6857613B2 JP 6857613 B2 JP6857613 B2 JP 6857613B2 JP 2017551685 A JP2017551685 A JP 2017551685A JP 2017551685 A JP2017551685 A JP 2017551685A JP 6857613 B2 JP6857613 B2 JP 6857613B2
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- 230000029983 protein stabilization Effects 0.000 title description 2
- 102000004169 proteins and genes Human genes 0.000 claims description 86
- 108090000623 proteins and genes Proteins 0.000 claims description 86
- 239000000203 mixture Substances 0.000 claims description 60
- 230000001225 therapeutic effect Effects 0.000 claims description 18
- 238000000034 method Methods 0.000 claims description 15
- 239000000845 maltitol Substances 0.000 claims description 14
- 235000010449 maltitol Nutrition 0.000 claims description 14
- VQHSOMBJVWLPSR-WUJBLJFYSA-N maltitol Chemical compound OC[C@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O VQHSOMBJVWLPSR-WUJBLJFYSA-N 0.000 claims description 14
- 229940035436 maltitol Drugs 0.000 claims description 14
- 108010019077 beta-Amylase Proteins 0.000 claims description 13
- 238000010438 heat treatment Methods 0.000 claims description 10
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 claims description 8
- 229930195725 Mannitol Natural products 0.000 claims description 8
- 239000000594 mannitol Substances 0.000 claims description 8
- 235000010355 mannitol Nutrition 0.000 claims description 8
- 238000003860 storage Methods 0.000 claims description 7
- 239000003381 stabilizer Substances 0.000 claims description 5
- TVXBFESIOXBWNM-UHFFFAOYSA-N Xylitol Natural products OCCC(O)C(O)C(O)CCO TVXBFESIOXBWNM-UHFFFAOYSA-N 0.000 claims description 4
- HEBKCHPVOIAQTA-UHFFFAOYSA-N meso ribitol Natural products OCC(O)C(O)C(O)CO HEBKCHPVOIAQTA-UHFFFAOYSA-N 0.000 claims description 4
- 239000000811 xylitol Substances 0.000 claims description 4
- HEBKCHPVOIAQTA-SCDXWVJYSA-N xylitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)CO HEBKCHPVOIAQTA-SCDXWVJYSA-N 0.000 claims description 4
- 235000010447 xylitol Nutrition 0.000 claims description 4
- 229960002675 xylitol Drugs 0.000 claims description 4
- 238000004108 freeze drying Methods 0.000 claims description 3
- 238000002156 mixing Methods 0.000 claims description 3
- 230000000087 stabilizing effect Effects 0.000 claims description 3
- 235000018102 proteins Nutrition 0.000 claims 1
- 150000003077 polyols Chemical class 0.000 description 55
- 229920005862 polyol Polymers 0.000 description 45
- 125000004432 carbon atom Chemical group C* 0.000 description 37
- 235000000346 sugar Nutrition 0.000 description 19
- 238000003556 assay Methods 0.000 description 13
- 230000000694 effects Effects 0.000 description 12
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 10
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 10
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 10
- 229940124272 protein stabilizer Drugs 0.000 description 10
- 230000002195 synergetic effect Effects 0.000 description 9
- 239000007788 liquid Substances 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 150000001413 amino acids Chemical class 0.000 description 6
- 150000008163 sugars Chemical class 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 239000000654 additive Substances 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 102000014914 Carrier Proteins Human genes 0.000 description 4
- 108010078791 Carrier Proteins Proteins 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- 238000004925 denaturation Methods 0.000 description 4
- 230000036425 denaturation Effects 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 3
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 241000209140 Triticum Species 0.000 description 3
- 235000021307 Triticum Nutrition 0.000 description 3
- 230000000996 additive effect Effects 0.000 description 3
- 239000000084 colloidal system Substances 0.000 description 3
- 150000002016 disaccharides Chemical group 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 239000000600 sorbitol Substances 0.000 description 3
- 235000010356 sorbitol Nutrition 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 2
- 229920000858 Cyclodextrin Polymers 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 229940097362 cyclodextrins Drugs 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 229940102223 injectable solution Drugs 0.000 description 2
- 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 2
- 239000000463 material Substances 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- -1 C12 polyol Chemical class 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- RGHNJXZEOKUKBD-SQOUGZDYSA-M D-gluconate Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O RGHNJXZEOKUKBD-SQOUGZDYSA-M 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 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 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108010029660 Intrinsically Disordered Proteins Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 108091007735 digestive proteases Proteins 0.000 description 1
- 230000003467 diminishing effect Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 229940050410 gluconate Drugs 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000002641 glycemic effect Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 230000005661 hydrophobic surface Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000002357 osmotic agent Substances 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- AKHNMLFCWUSKQB-UHFFFAOYSA-L sodium thiosulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=S AKHNMLFCWUSKQB-UHFFFAOYSA-L 0.000 description 1
- 235000019345 sodium thiosulphate Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/14—Prodigestives, e.g. acids, enzymes, appetite stimulants, antidyspeptics, tonics, antiflatulents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01002—Beta-amylase (3.2.1.2)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Crystallography & Structural Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nutrition Science (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Peptides Or Proteins (AREA)
Description
)12個の炭素原子からなる第1のポリオール、優先的に、マルチトールと、(ii)4〜6個の炭素原子からなる第2のポリオール、優先的に、ソルビトール、キシリトール及び/又はマンニトールとの組合せからなる。
− 論文Cicerone MT;Tellington A;Trost l;Sokolov A.Substantially improved stability
of biological agents in dried form:The role of glassy dynamics in preservation of biopharmaceuticals.BioProc.Int.1:36−47(2003)。
− 二糖、二糖誘導体、担体タンパク質及び多糖から構成される添加剤を記載している特許出願国際公開第98/00530号パンフレット。
− 典型的にグルコース及びNaClを含む浸透圧剤(osmotic agent);
− pH調節剤、例えばラクテート又はグルコネートタイプの緩衝系;
− 本発明に係る組合せ以外のタンパク質安定剤、例えばリジン及びアルギニンなどのアミノ酸、担体タンパク質、親水コロイド、界面活性剤、又は天然もしくは修飾シクロデキストリン。
滴定アッセイにより、酵素活性を測定した。活性の低下のパーセンテージを、各アッセイの熱処理前に得られる活性の測定値から計算した。
Claims (5)
- β−アミラーゼ安定剤としての、マルチトールと、キシリトール及びマンニトールから選択される1種以上と、の組合せであって、前記キシリトール及びマンニトールから選択される1種以上に対する前記マルチトールの乾燥重量比が5/95〜95/5の範囲である組合せの使用。
- 低温化及び/又は凍結乾燥処理及び/又は貯蔵、特に、溶液中での貯蔵、及び/又は特に加熱による、特に溶液中での加熱による熱処理に供されるβ−アミラーゼを安定させるための、請求項1に記載の使用。
- タンパク質と、マルチトールと、マンニトールと、を含み、
前記マンニトールに対する前記マルチトールの乾燥重量比が5/95〜95/5の範囲である、β−アミラーゼ組成物。 - 治療用β−アミラーゼ組成物又は工業使用が意図されたβ−アミラーゼ組成物から選択される、請求項3に記載のβ−アミラーゼ組成物。
- 請求項3又は4に記載の組成物を調製するための方法において、β−アミラーゼ、マルチトール及びマンニトールを一緒に混合する工程を含むことを特徴とする方法。
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR1552899A FR3034418B1 (fr) | 2015-04-03 | 2015-04-03 | Utilisation de combinaisons particulieres de carbohydrates pour stabiliser des proteines, et compositions proteiques contenant de telles combinaisons |
FR1552899 | 2015-04-03 | ||
PCT/FR2016/050709 WO2016156734A1 (fr) | 2015-04-03 | 2016-03-30 | Stabilisation de proteines |
Publications (3)
Publication Number | Publication Date |
---|---|
JP2018516239A JP2018516239A (ja) | 2018-06-21 |
JP2018516239A5 JP2018516239A5 (ja) | 2019-03-07 |
JP6857613B2 true JP6857613B2 (ja) | 2021-04-14 |
Family
ID=53483991
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2017551685A Active JP6857613B2 (ja) | 2015-04-03 | 2016-03-30 | タンパク質の安定化 |
Country Status (7)
Country | Link |
---|---|
US (1) | US10822372B2 (ja) |
EP (1) | EP3277702B1 (ja) |
JP (1) | JP6857613B2 (ja) |
CN (1) | CN107531747A (ja) |
DK (1) | DK3277702T3 (ja) |
FR (1) | FR3034418B1 (ja) |
WO (1) | WO2016156734A1 (ja) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP7039308B2 (ja) * | 2017-02-08 | 2022-03-22 | 三洋化成工業株式会社 | 細胞培養用担体 |
CN108424035A (zh) * | 2018-04-19 | 2018-08-21 | 中原工学院 | 一种聚合物水泥发泡剂及其发泡混凝土的制备方法 |
Family Cites Families (16)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0779694B2 (ja) | 1985-07-09 | 1995-08-30 | カドラント バイオリソ−シズ リミテツド | 蛋白質および同類品の保護 |
GB9010742D0 (en) * | 1990-05-14 | 1990-07-04 | Quadrant Bioresources Ltd | Stabilization of biological macromolecular substances |
CA2177429A1 (en) * | 1995-06-29 | 1996-12-30 | Charles Allen Rodgers | Reduced fat cheese-flavored snack filling |
US5876992A (en) * | 1996-07-03 | 1999-03-02 | Molecular Biology Resources, Inc. | Method and formulation for stabilization of enzymes |
AU3957400A (en) * | 1999-04-16 | 2000-11-02 | Novo Nordisk A/S | Dry, mouldable drug formulation |
FI20021312A (fi) * | 2002-07-03 | 2004-01-04 | Danisco Sweeteners Oy | Polyolikoostumusten kiteyttäminen, kiteinen polyolikoostumustuote ja sen käyttö |
CA2498014C (en) * | 2002-09-11 | 2011-11-29 | Puratos, Naamloze Vennootschap | Use of family 8 enzymes with xylanolytic activity in baking |
EP1574567A1 (en) * | 2004-03-11 | 2005-09-14 | Puratos Naamloze Vennootschap | Novel xylanases and their use |
JP5275803B2 (ja) * | 2005-09-16 | 2013-08-28 | メリアル リミテッド | 凍結乾燥ワクチン用安定剤 |
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AU2012314515B2 (en) * | 2011-09-26 | 2018-03-15 | Preanalytix Gmbh | Stabilisation and isolation of extracellular nucleic acids |
CN102533689A (zh) * | 2011-12-30 | 2012-07-04 | 华东师范大学 | 一种谷氨酰胺转胺酶真空干燥的制备方法 |
CN103159839B (zh) * | 2013-03-28 | 2014-07-30 | 云南天保桦生物资源开发有限公司 | 热稳定保护的α-淀粉酶抑制剂及其用途 |
WO2015021600A1 (en) * | 2013-08-13 | 2015-02-19 | Danisco Us Inc. | Beta-amylase and methods of use |
CN104099313B (zh) * | 2014-07-18 | 2016-04-06 | 天津天绿健科技有限公司 | 一种啤酒液体复配酶 |
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DK3277702T3 (da) | 2023-12-04 |
WO2016156734A1 (fr) | 2016-10-06 |
JP2018516239A (ja) | 2018-06-21 |
US10822372B2 (en) | 2020-11-03 |
FR3034418B1 (fr) | 2018-09-28 |
US20180118779A1 (en) | 2018-05-03 |
CN107531747A (zh) | 2018-01-02 |
EP3277702B1 (fr) | 2023-09-06 |
EP3277702A1 (fr) | 2018-02-07 |
FR3034418A1 (fr) | 2016-10-07 |
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