JPS608226A - 低分子蛋白質を有効成分とする制ガン剤 - Google Patents
低分子蛋白質を有効成分とする制ガン剤Info
- Publication number
- JPS608226A JPS608226A JP58117949A JP11794983A JPS608226A JP S608226 A JPS608226 A JP S608226A JP 58117949 A JP58117949 A JP 58117949A JP 11794983 A JP11794983 A JP 11794983A JP S608226 A JPS608226 A JP S608226A
- Authority
- JP
- Japan
- Prior art keywords
- solution
- recovery rate
- degree
- purification
- amino acid
- 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.)
- Granted
Links
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 41
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 41
- 238000000034 method Methods 0.000 claims abstract description 90
- 239000000243 solution Substances 0.000 claims abstract description 43
- 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 claims abstract description 34
- 150000001413 amino acids Chemical class 0.000 claims abstract description 18
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims abstract description 15
- 239000000203 mixture Substances 0.000 claims abstract description 12
- 238000006243 chemical reaction Methods 0.000 claims abstract description 11
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 claims abstract description 6
- 239000007864 aqueous solution Substances 0.000 claims abstract description 3
- OHJMTUPIZMNBFR-UHFFFAOYSA-N biuret Chemical compound NC(=O)NC(N)=O OHJMTUPIZMNBFR-UHFFFAOYSA-N 0.000 claims abstract description 3
- 230000002378 acidificating effect Effects 0.000 claims abstract 2
- 230000007062 hydrolysis Effects 0.000 claims abstract 2
- 238000006460 hydrolysis reaction Methods 0.000 claims abstract 2
- 239000000126 substance Substances 0.000 claims description 60
- 239000000872 buffer Substances 0.000 claims description 52
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 4
- 238000010521 absorption reaction Methods 0.000 claims description 3
- 238000001556 precipitation Methods 0.000 claims description 3
- 238000005903 acid hydrolysis reaction Methods 0.000 claims description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 abstract description 35
- 210000002966 serum Anatomy 0.000 abstract description 27
- 229910052921 ammonium sulfate Inorganic materials 0.000 abstract description 26
- 235000011130 ammonium sulphate Nutrition 0.000 abstract description 26
- 239000007853 buffer solution Substances 0.000 abstract description 18
- 238000002523 gelfiltration Methods 0.000 abstract description 18
- 210000004369 blood Anatomy 0.000 abstract description 15
- 239000008280 blood Substances 0.000 abstract description 15
- 229910052588 hydroxylapatite Inorganic materials 0.000 abstract description 9
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 abstract description 9
- 238000005185 salting out Methods 0.000 abstract description 9
- 239000000463 material Substances 0.000 abstract description 7
- 238000012360 testing method Methods 0.000 abstract description 7
- 241001465754 Metazoa Species 0.000 abstract description 6
- 239000002246 antineoplastic agent Substances 0.000 abstract description 4
- 238000004587 chromatography analysis Methods 0.000 abstract description 4
- 238000004440 column chromatography Methods 0.000 abstract description 3
- 238000004090 dissolution Methods 0.000 abstract description 3
- -1 gel filtration Chemical compound 0.000 abstract description 2
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 abstract description 2
- 238000002360 preparation method Methods 0.000 abstract description 2
- 230000000694 effects Effects 0.000 description 110
- 238000011084 recovery Methods 0.000 description 84
- 238000000746 purification Methods 0.000 description 69
- 210000004027 cell Anatomy 0.000 description 40
- 238000000108 ultra-filtration Methods 0.000 description 39
- 238000000502 dialysis Methods 0.000 description 28
- 239000008363 phosphate buffer Substances 0.000 description 19
- 239000002244 precipitate Substances 0.000 description 19
- 238000010828 elution Methods 0.000 description 15
- 239000002158 endotoxin Substances 0.000 description 14
- 230000001472 cytotoxic effect Effects 0.000 description 13
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 12
- 238000004519 manufacturing process Methods 0.000 description 12
- 210000003462 vein Anatomy 0.000 description 12
- 238000005406 washing Methods 0.000 description 12
- 241000283973 Oryctolagus cuniculus Species 0.000 description 10
- 238000005119 centrifugation Methods 0.000 description 10
- 231100000433 cytotoxic Toxicity 0.000 description 10
- 238000001914 filtration Methods 0.000 description 10
- 241000699670 Mus sp. Species 0.000 description 9
- 206010028980 Neoplasm Diseases 0.000 description 9
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 9
- 239000004202 carbamide Substances 0.000 description 9
- 239000012528 membrane Substances 0.000 description 9
- 230000001766 physiological effect Effects 0.000 description 9
- 239000000725 suspension Substances 0.000 description 9
- 239000013543 active substance Substances 0.000 description 8
- 239000007788 liquid Substances 0.000 description 8
- 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 8
- 239000006228 supernatant Substances 0.000 description 8
- 201000011510 cancer Diseases 0.000 description 7
- 239000012141 concentrate Substances 0.000 description 7
- 238000001962 electrophoresis Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 6
- 241000186216 Corynebacterium Species 0.000 description 6
- 108010052832 Cytochromes Proteins 0.000 description 6
- 102000018832 Cytochromes Human genes 0.000 description 6
- 108090001090 Lectins Proteins 0.000 description 6
- 102000004856 Lectins Human genes 0.000 description 6
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 239000002523 lectin Substances 0.000 description 6
- 239000011734 sodium Substances 0.000 description 6
- 239000001488 sodium phosphate Substances 0.000 description 6
- 229910000162 sodium phosphate Inorganic materials 0.000 description 6
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 6
- 229910019142 PO4 Inorganic materials 0.000 description 5
- 239000000385 dialysis solution Substances 0.000 description 5
- 238000005194 fractionation Methods 0.000 description 5
- 230000003308 immunostimulating effect Effects 0.000 description 5
- 230000017074 necrotic cell death Effects 0.000 description 5
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 5
- 239000010452 phosphate Substances 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- 230000000259 anti-tumor effect Effects 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 239000002198 insoluble material Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 4
- 229960005322 streptomycin Drugs 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 208000011691 Burkitt lymphomas Diseases 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 229930182555 Penicillin Natural products 0.000 description 3
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound 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 3
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 3
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 3
- 208000005718 Stomach Neoplasms Diseases 0.000 description 3
- 230000000975 bioactive effect Effects 0.000 description 3
- 239000001569 carbon dioxide Substances 0.000 description 3
- 229910002092 carbon dioxide Inorganic materials 0.000 description 3
- 230000022534 cell killing Effects 0.000 description 3
- 239000006285 cell suspension Substances 0.000 description 3
- 206010017758 gastric cancer Diseases 0.000 description 3
- 230000002008 hemorrhagic effect Effects 0.000 description 3
- 229920006008 lipopolysaccharide Polymers 0.000 description 3
- 238000000691 measurement method Methods 0.000 description 3
- 229940049954 penicillin Drugs 0.000 description 3
- 230000000144 pharmacologic effect Effects 0.000 description 3
- 229910052698 phosphorus Inorganic materials 0.000 description 3
- 239000011574 phosphorus Substances 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 229910052938 sodium sulfate Inorganic materials 0.000 description 3
- 235000011152 sodium sulphate Nutrition 0.000 description 3
- 201000011549 stomach cancer Diseases 0.000 description 3
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 2
- 108010038061 Chymotrypsinogen Proteins 0.000 description 2
- 101710101803 DNA-binding protein J Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 239000006145 Eagle's minimal essential medium Substances 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241000186779 Listeria monocytogenes Species 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 241000186359 Mycobacterium Species 0.000 description 2
- 241000283977 Oryctolagus Species 0.000 description 2
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 229920000392 Zymosan Polymers 0.000 description 2
- 230000007059 acute toxicity Effects 0.000 description 2
- 231100000403 acute toxicity Toxicity 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000001093 anti-cancer Effects 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 210000005252 bulbus oculi Anatomy 0.000 description 2
- 208000025188 carcinoma of pharynx Diseases 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000012045 crude solution Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 231100000053 low toxicity Toxicity 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 108010001062 polysaccharide-K Proteins 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 108010048090 soybean lectin Proteins 0.000 description 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 description 1
- 102000002281 Adenylate kinase Human genes 0.000 description 1
- 108020000543 Adenylate kinase Proteins 0.000 description 1
- 206010002091 Anaesthesia Diseases 0.000 description 1
- 101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 244000045232 Canavalia ensiformis Species 0.000 description 1
- 235000010520 Canavalia ensiformis Nutrition 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 241000186427 Cutibacterium acnes Species 0.000 description 1
- 108010007529 Cytochromes c2 Proteins 0.000 description 1
- 241001669680 Dormitator maculatus Species 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000187678 Nocardia asteroides Species 0.000 description 1
- 208000009565 Pharyngeal Neoplasms Diseases 0.000 description 1
- 206010034811 Pharyngeal cancer Diseases 0.000 description 1
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 1
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 1
- 241001040659 Plasmodium (Plasmodium) Species 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 241000293871 Salmonella enterica subsp. enterica serovar Typhi Species 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 241000193996 Streptococcus pyogenes Species 0.000 description 1
- 101710117064 Trimethylamine corrinoid protein 1 Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 240000001417 Vigna umbellata Species 0.000 description 1
- 235000011453 Vigna umbellata Nutrition 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 230000003187 abdominal effect Effects 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 238000001467 acupuncture Methods 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005266 casting Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 108010018850 cytochrome C(551) Proteins 0.000 description 1
- 108010039340 cytochrome C5 Proteins 0.000 description 1
- 230000000445 cytocidal effect Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 238000002784 cytotoxicity assay Methods 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 231100000517 death Toxicity 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 231100000566 intoxication Toxicity 0.000 description 1
- 230000035987 intoxication Effects 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 230000001338 necrotic effect Effects 0.000 description 1
- PGSADBUBUOPOJS-UHFFFAOYSA-N neutral red Chemical compound Cl.C1=C(C)C(N)=CC2=NC3=CC(N(C)C)=CC=C3N=C21 PGSADBUBUOPOJS-UHFFFAOYSA-N 0.000 description 1
- 238000011197 physicochemical method Methods 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 229940055019 propionibacterium acne Drugs 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP58117949A JPS608226A (ja) | 1983-06-28 | 1983-06-28 | 低分子蛋白質を有効成分とする制ガン剤 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP58117949A JPS608226A (ja) | 1983-06-28 | 1983-06-28 | 低分子蛋白質を有効成分とする制ガン剤 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS608226A true JPS608226A (ja) | 1985-01-17 |
JPH0322851B2 JPH0322851B2 (enrdf_load_stackoverflow) | 1991-03-27 |
Family
ID=14724217
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP58117949A Granted JPS608226A (ja) | 1983-06-28 | 1983-06-28 | 低分子蛋白質を有効成分とする制ガン剤 |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS608226A (enrdf_load_stackoverflow) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2601678A1 (fr) * | 1986-07-18 | 1988-01-22 | Inst Nat Sante Rech Med | Peptides comprenant la sequence seryl-aspartyl-lysyl-prolyle, procede pour l'extraction du tetrapeptide correspondant, et applications, notamment a la protection de la moelle osseuse au cours de traitements anticancereux par la chimiotherapie |
JPS63115732A (ja) * | 1986-11-04 | 1988-05-20 | 株式会社 磯輪鉄工所 | 段ボ−ル製造装置の自動フル−ト変更装置 |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS59118714A (ja) * | 1982-12-24 | 1984-07-09 | Otsuka Pharmaceut Co Ltd | 制ガン作用を有する低分子蛋白質 |
-
1983
- 1983-06-28 JP JP58117949A patent/JPS608226A/ja active Granted
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS59118714A (ja) * | 1982-12-24 | 1984-07-09 | Otsuka Pharmaceut Co Ltd | 制ガン作用を有する低分子蛋白質 |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2601678A1 (fr) * | 1986-07-18 | 1988-01-22 | Inst Nat Sante Rech Med | Peptides comprenant la sequence seryl-aspartyl-lysyl-prolyle, procede pour l'extraction du tetrapeptide correspondant, et applications, notamment a la protection de la moelle osseuse au cours de traitements anticancereux par la chimiotherapie |
JPS63115732A (ja) * | 1986-11-04 | 1988-05-20 | 株式会社 磯輪鉄工所 | 段ボ−ル製造装置の自動フル−ト変更装置 |
Also Published As
Publication number | Publication date |
---|---|
JPH0322851B2 (enrdf_load_stackoverflow) | 1991-03-27 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JPS5943929B2 (ja) | 多糖体rbs物質,その製法およびそれを有効成分とする抗腫瘍性剤 | |
US4845078A (en) | Method for treating hematopoietic diseases | |
US3945889A (en) | Preparation of human placental hyaluronidase | |
JPS5896025A (ja) | 新規生理活性物質ch−1およびその製造法 | |
EP0132125B1 (en) | A protein having antitumor activity | |
NO146818B (no) | Fremgangsmaate for aa danne kanaler med hoey fluidumledningsevne i en formasjon rundt et borehull | |
US4104125A (en) | Process for producing human lysozyme | |
JPS608226A (ja) | 低分子蛋白質を有効成分とする制ガン剤 | |
JPS58148824A (ja) | 線溶活性物質の製造法 | |
EP0246861B1 (en) | Use of compositions based on crotoxine, for the manufacture of a medicament for the treatment of carcinomas | |
US3905870A (en) | Purification of kallikrein | |
SU871721A3 (ru) | Способ получени биологически активного вещества,обладающего способностью усиливать секрецию инсулина и улучшать глюкозную толерантность | |
JPS59141519A (ja) | 制ガン作用を有する蛋白質 | |
JPS59118714A (ja) | 制ガン作用を有する低分子蛋白質 | |
JPS5930686B2 (ja) | 免疫制御作用を有するペプタイドの製造方法 | |
JPS59118715A (ja) | 制ガン作用を有する低分子蛋白質 | |
JPS5822445B2 (ja) | 安定な固体の人血漿コリンエステラ−ゼ製剤の製法 | |
SE455163B (sv) | Uropepsin for anvendning som terapeutikum mot allergiska sjukdomar, immunkomplexsjukdomar och tumorer | |
JPS63164895A (ja) | 培養細胞由来のレクチン様蛋白質及びその製法並びに該物質を主成分とする抗腫瘍剤 | |
JPS59118716A (ja) | 制ガン作用を有する低分子蛋白質 | |
JPH0525055A (ja) | 血圧降下剤 | |
JPH0381291A (ja) | トリペプチド | |
JPS62258324A (ja) | 制ガン作用を有する糖蛋白質 | |
JPS59170018A (ja) | 感染症予防治療剤 | |
JPS6137730A (ja) | 制ガン作用を有する蛋白質 |