JPS6363559B2 - - Google Patents
Info
- Publication number
- JPS6363559B2 JPS6363559B2 JP56209841A JP20984181A JPS6363559B2 JP S6363559 B2 JPS6363559 B2 JP S6363559B2 JP 56209841 A JP56209841 A JP 56209841A JP 20984181 A JP20984181 A JP 20984181A JP S6363559 B2 JPS6363559 B2 JP S6363559B2
- Authority
- JP
- Japan
- Prior art keywords
- active substance
- physiologically active
- buffer
- salt concentration
- mammal
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 239000013543 active substance Substances 0.000 claims description 45
- 239000000872 buffer Substances 0.000 claims description 35
- 238000000034 method Methods 0.000 claims description 22
- 238000000746 purification Methods 0.000 claims description 16
- 239000002158 endotoxin Substances 0.000 claims description 15
- 239000007853 buffer solution Substances 0.000 claims description 14
- 150000003839 salts Chemical class 0.000 claims description 14
- 150000001450 anions Chemical class 0.000 claims description 13
- 241000124008 Mammalia Species 0.000 claims description 12
- 238000002523 gelfiltration Methods 0.000 claims description 12
- 239000000126 substance Substances 0.000 claims description 11
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 9
- 230000001093 anti-cancer Effects 0.000 claims description 9
- 239000012045 crude solution Substances 0.000 claims description 8
- 210000000865 mononuclear phagocyte system Anatomy 0.000 claims description 6
- 241000894007 species Species 0.000 claims description 6
- 241000894006 Bacteria Species 0.000 claims description 5
- 210000002540 macrophage Anatomy 0.000 claims description 5
- 238000001042 affinity chromatography Methods 0.000 claims description 4
- 230000003213 activating effect Effects 0.000 claims description 3
- 238000001179 sorption measurement Methods 0.000 claims description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 42
- 210000002966 serum Anatomy 0.000 description 24
- 230000000694 effects Effects 0.000 description 23
- 239000011780 sodium chloride Substances 0.000 description 20
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 19
- 206010028980 Neoplasm Diseases 0.000 description 12
- 210000004027 cell Anatomy 0.000 description 12
- 239000012264 purified product Substances 0.000 description 12
- 238000011084 recovery Methods 0.000 description 12
- 239000000243 solution Substances 0.000 description 10
- 241000699670 Mus sp. Species 0.000 description 9
- 230000017074 necrotic cell death Effects 0.000 description 8
- 229920002271 DEAE-Sepharose Polymers 0.000 description 7
- 210000002381 plasma Anatomy 0.000 description 7
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 238000010828 elution Methods 0.000 description 6
- 230000002008 hemorrhagic effect Effects 0.000 description 6
- 239000008363 phosphate buffer Substances 0.000 description 6
- 239000012506 Sephacryl® Substances 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000000108 ultra-filtration Methods 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 241000186427 Cutibacterium acnes Species 0.000 description 4
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 4
- 229920005654 Sephadex Polymers 0.000 description 4
- 239000012507 Sephadex™ Substances 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 230000022534 cell killing Effects 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 239000002504 physiological saline solution Substances 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 3
- 108010088751 Albumins Proteins 0.000 description 3
- 102000009027 Albumins Human genes 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 206010039491 Sarcoma Diseases 0.000 description 3
- YKCWQPZFAFZLBI-UHFFFAOYSA-N cibacron blue Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC=C1S(O)(=O)=O YKCWQPZFAFZLBI-UHFFFAOYSA-N 0.000 description 3
- 239000006167 equilibration buffer Substances 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 229920006008 lipopolysaccharide Polymers 0.000 description 3
- 229940055019 propionibacterium acne Drugs 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 210000003462 vein Anatomy 0.000 description 3
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 2
- 238000011740 C57BL/6 mouse Methods 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 241000186216 Corynebacterium Species 0.000 description 2
- 241001464975 Cutibacterium granulosum Species 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 241000192125 Firmicutes Species 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 210000000601 blood cell Anatomy 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000000445 cytocidal effect Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 238000007865 diluting Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 230000001766 physiological effect Effects 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 102000002572 Alpha-Globulins Human genes 0.000 description 1
- 108010068307 Alpha-Globulins Proteins 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 239000006145 Eagle's minimal essential medium Substances 0.000 description 1
- 241001653121 Glenoides Species 0.000 description 1
- OWYWGLHRNBIFJP-UHFFFAOYSA-N Ipazine Chemical compound CCN(CC)C1=NC(Cl)=NC(NC(C)C)=N1 OWYWGLHRNBIFJP-UHFFFAOYSA-N 0.000 description 1
- 241000186359 Mycobacterium Species 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 241000187654 Nocardia Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical group N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 1
- JQYMGXZJTCOARG-UHFFFAOYSA-N Reactive blue 2 Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC(S(O)(=O)=O)=C1 JQYMGXZJTCOARG-UHFFFAOYSA-N 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 241000936695 Streptomyces gardneri Species 0.000 description 1
- 241000223997 Toxoplasma gondii Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 208000037386 Typhoid Diseases 0.000 description 1
- 229920000392 Zymosan Polymers 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 229940088623 biologically active substance Drugs 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 230000005907 cancer growth Effects 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 229920002301 cellulose acetate Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 231100000409 cytocidal Toxicity 0.000 description 1
- 239000003145 cytotoxic factor Substances 0.000 description 1
- 125000001664 diethylamino group Chemical group [H]C([H])([H])C([H])([H])N(*)C([H])([H])C([H])([H])[H] 0.000 description 1
- 239000012470 diluted sample Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 210000000416 exudates and transudate Anatomy 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000012145 high-salt buffer Substances 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 210000004880 lymph fluid Anatomy 0.000 description 1
- 201000004792 malaria Diseases 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 230000001338 necrotic effect Effects 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 201000008297 typhoid fever Diseases 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP56209841A JPS57140726A (en) | 1981-12-28 | 1981-12-28 | Purification of physiologically active substance having carcinostatic action |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP56209841A JPS57140726A (en) | 1981-12-28 | 1981-12-28 | Purification of physiologically active substance having carcinostatic action |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP55143197 Division |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS57140726A JPS57140726A (en) | 1982-08-31 |
JPS6363559B2 true JPS6363559B2 (fr) | 1988-12-07 |
Family
ID=16579502
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP56209841A Granted JPS57140726A (en) | 1981-12-28 | 1981-12-28 | Purification of physiologically active substance having carcinostatic action |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS57140726A (fr) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU8956582A (en) * | 1982-10-06 | 1984-04-24 | Makitsubo, T. | Process for extracting tumor necrosis factor from macrophage |
JPH088873B2 (ja) * | 1983-07-28 | 1996-01-31 | 大日本製薬株式会社 | ヒト癌壊死因子の製造法 |
-
1981
- 1981-12-28 JP JP56209841A patent/JPS57140726A/ja active Granted
Also Published As
Publication number | Publication date |
---|---|
JPS57140726A (en) | 1982-08-31 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JPS6363558B2 (fr) | ||
US5372942A (en) | Protease K resistant arginine deiminase, its method of preparation and its use as an anti-neoplastic agent | |
US4529594A (en) | Protein having antitumor activity | |
US4845078A (en) | Method for treating hematopoietic diseases | |
JPS6363559B2 (fr) | ||
US5114710A (en) | M-csf as a therapeutic agent for thrombocytopenia | |
Johnson | Simplified procedure for removing non-specific staining components from fluorescein-labelled conjugates | |
US5023320A (en) | Process for the purification of physiologically active substance having antitumor activity | |
US5244807A (en) | Production of pseudomonas xa cells containing indolyl-3-alkane alpha-hydroxylase | |
JPS6019720A (ja) | ヒト内来性癌制御因子およびその製造法 | |
KR890004692B1 (ko) | 항종양 생리학적 활성물질의 정제방법 | |
JPH0341478B2 (fr) | ||
JPS60243018A (ja) | ヒト内来性癌制御因子 | |
JPS597695B2 (ja) | 免疫制御作用を有するペプタイド製剤 | |
JPH0479358B2 (fr) | ||
JPH0322851B2 (fr) | ||
JPS60226816A (ja) | 抗腫瘍活性をもつヒト由来蛋白質 | |
JPS59118715A (ja) | 制ガン作用を有する低分子蛋白質 | |
JPS59118714A (ja) | 制ガン作用を有する低分子蛋白質 | |
JPS5982315A (ja) | 腫瘍壊死因子の製造法 | |
JPH0566960B2 (fr) | ||
JPS61207334A (ja) | 腫瘍細胞障害性物質 | |
JPS6272623A (ja) | 悪性腫瘍等の治療方法 | |
JPS62103021A (ja) | 細胞障害作用を有する生理活性物質およびその製造方法 | |
JPS6169797A (ja) | 蛋白質物質 |