IL46587A - Process for the isolation of a polyvalent proteinase inhibitor - Google Patents
Process for the isolation of a polyvalent proteinase inhibitorInfo
- Publication number
- IL46587A IL46587A IL46587A IL4658775A IL46587A IL 46587 A IL46587 A IL 46587A IL 46587 A IL46587 A IL 46587A IL 4658775 A IL4658775 A IL 4658775A IL 46587 A IL46587 A IL 46587A
- Authority
- IL
- Israel
- Prior art keywords
- proteinase inhibitor
- sulfonic acid
- inhibitor
- adsorbant
- polystyrene
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 27
- 239000000137 peptide hydrolase inhibitor Substances 0.000 title claims description 21
- 238000002955 isolation Methods 0.000 title claims description 10
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 17
- 239000003112 inhibitor Substances 0.000 claims description 15
- 229920001577 copolymer Polymers 0.000 claims description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 12
- 238000010828 elution Methods 0.000 claims description 11
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 claims description 10
- 239000011347 resin Substances 0.000 claims description 10
- 229920005989 resin Polymers 0.000 claims description 10
- 239000000243 solution Substances 0.000 claims description 10
- 150000002500 ions Chemical class 0.000 claims description 9
- 239000011780 sodium chloride Substances 0.000 claims description 9
- 229940117913 acrylamide Drugs 0.000 claims description 8
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 claims description 7
- 150000003839 salts Chemical class 0.000 claims description 7
- 238000001179 sorption measurement Methods 0.000 claims description 7
- NLVXSWCKKBEXTG-UHFFFAOYSA-M ethenesulfonate Chemical compound [O-]S(=O)(=O)C=C NLVXSWCKKBEXTG-UHFFFAOYSA-M 0.000 claims description 6
- 210000001557 animal structure Anatomy 0.000 claims description 4
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical group OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 claims description 3
- 239000007864 aqueous solution Substances 0.000 claims description 3
- 229920001467 poly(styrenesulfonates) Polymers 0.000 claims description 3
- 229940005642 polystyrene sulfonic acid Drugs 0.000 claims description 3
- NLVXSWCKKBEXTG-UHFFFAOYSA-N vinylsulfonic acid Chemical compound OS(=O)(=O)C=C NLVXSWCKKBEXTG-UHFFFAOYSA-N 0.000 claims description 3
- 238000004132 cross linking Methods 0.000 claims description 2
- 239000004793 Polystyrene Substances 0.000 claims 2
- 229920002223 polystyrene Polymers 0.000 claims 2
- -1 sulfonic acid ion Chemical class 0.000 claims 2
- 238000007334 copolymerization reaction Methods 0.000 claims 1
- 239000012266 salt solution Substances 0.000 claims 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 claims 1
- 239000002253 acid Substances 0.000 description 12
- 239000000284 extract Substances 0.000 description 7
- 239000001768 carboxy methyl cellulose Substances 0.000 description 6
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 6
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 6
- 229940105329 carboxymethylcellulose Drugs 0.000 description 6
- 229940012957 plasmin Drugs 0.000 description 6
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 239000000047 product Substances 0.000 description 4
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 210000004072 lung Anatomy 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 description 2
- 235000010262 sodium metabisulphite Nutrition 0.000 description 2
- 125000000542 sulfonic acid group Chemical group 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- UEZVMMHDMIWARA-UHFFFAOYSA-N Metaphosphoric acid Chemical compound OP(=O)=O UEZVMMHDMIWARA-UHFFFAOYSA-N 0.000 description 1
- XBDQKXXYIPTUBI-UHFFFAOYSA-N Propionic acid Substances CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 1
- 101710102734 Proteinase inhibitor A Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 229920006322 acrylamide copolymer Polymers 0.000 description 1
- 230000000274 adsorptive effect Effects 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 239000006286 aqueous extract Substances 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000008098 formaldehyde solution Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- RPACBEVZENYWOL-XFULWGLBSA-M sodium;(2r)-2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate Chemical compound [Na+].C=1C=C(Cl)C=CC=1OCCCCCC[C@]1(C(=O)[O-])CO1 RPACBEVZENYWOL-XFULWGLBSA-M 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- NBOMNTLFRHMDEZ-UHFFFAOYSA-N thiosalicylic acid Chemical compound OC(=O)C1=CC=CC=C1S NBOMNTLFRHMDEZ-UHFFFAOYSA-N 0.000 description 1
- 229940103494 thiosalicylic acid Drugs 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8114—Kunitz type inhibitors
- C07K14/8117—Bovine/basic pancreatic trypsin inhibitor (BPTI, aprotinin)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE2406971A DE2406971B2 (de) | 1974-02-14 | 1974-02-14 | Verfahren zur Gewinnung eines polyvalenten Proteinasen-Inhibitors |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL46587A0 IL46587A0 (en) | 1975-04-25 |
| IL46587A true IL46587A (en) | 1977-06-30 |
Family
ID=5907334
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL46587A IL46587A (en) | 1974-02-14 | 1975-02-07 | Process for the isolation of a polyvalent proteinase inhibitor |
Country Status (14)
| Country | Link |
|---|---|
| JP (1) | JPS50111211A (da) |
| AT (1) | AT338414B (da) |
| BE (1) | BE825570A (da) |
| CH (1) | CH610909A5 (da) |
| DE (1) | DE2406971B2 (da) |
| DK (1) | DK145468B (da) |
| FR (1) | FR2261286B1 (da) |
| GB (1) | GB1493960A (da) |
| IE (1) | IE40600B1 (da) |
| IL (1) | IL46587A (da) |
| IT (1) | IT1043948B (da) |
| LU (1) | LU71826A1 (da) |
| NL (1) | NL7501488A (da) |
| SE (1) | SE7501654L (da) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2527222A1 (fr) * | 1982-05-19 | 1983-11-25 | Christine Fougnot | Procede de separation et de purification des proteases et des antiproteases de la coagulation sanguine, ainsi que du complexe protease/antiprotease |
-
1974
- 1974-02-14 DE DE2406971A patent/DE2406971B2/de not_active Ceased
-
1975
- 1975-02-07 NL NL7501488A patent/NL7501488A/xx not_active Application Discontinuation
- 1975-02-07 IL IL46587A patent/IL46587A/en unknown
- 1975-02-12 LU LU71826A patent/LU71826A1/xx unknown
- 1975-02-12 IT IT20216/75A patent/IT1043948B/it active
- 1975-02-13 CH CH174675A patent/CH610909A5/xx not_active IP Right Cessation
- 1975-02-13 AT AT107175A patent/AT338414B/de not_active IP Right Cessation
- 1975-02-13 DK DK52175AA patent/DK145468B/da not_active Application Discontinuation
- 1975-02-13 IE IE280/75A patent/IE40600B1/xx unknown
- 1975-02-13 JP JP50017517A patent/JPS50111211A/ja active Pending
- 1975-02-14 GB GB6296/75A patent/GB1493960A/en not_active Expired
- 1975-02-14 FR FR7504757A patent/FR2261286B1/fr not_active Expired
- 1975-02-14 SE SE7501654A patent/SE7501654L/ not_active Application Discontinuation
- 1975-02-14 BE BE153395A patent/BE825570A/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| NL7501488A (nl) | 1975-08-18 |
| JPS50111211A (da) | 1975-09-01 |
| CH610909A5 (en) | 1979-05-15 |
| ATA107175A (de) | 1976-12-15 |
| LU71826A1 (da) | 1976-12-31 |
| FR2261286A1 (da) | 1975-09-12 |
| BE825570A (fr) | 1975-08-14 |
| DE2406971B2 (de) | 1979-08-09 |
| IE40600B1 (en) | 1979-07-04 |
| IE40600L (en) | 1975-08-14 |
| DK52175A (da) | 1975-10-06 |
| GB1493960A (en) | 1977-12-07 |
| AT338414B (de) | 1977-08-25 |
| IT1043948B (it) | 1980-02-29 |
| IL46587A0 (en) | 1975-04-25 |
| FR2261286B1 (da) | 1979-04-06 |
| DE2406971A1 (de) | 1975-08-21 |
| DK145468B (da) | 1982-11-22 |
| SE7501654L (da) | 1975-08-15 |
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