JPS59118715A - 制ガン作用を有する低分子蛋白質 - Google Patents
制ガン作用を有する低分子蛋白質Info
- Publication number
- JPS59118715A JPS59118715A JP57233949A JP23394982A JPS59118715A JP S59118715 A JPS59118715 A JP S59118715A JP 57233949 A JP57233949 A JP 57233949A JP 23394982 A JP23394982 A JP 23394982A JP S59118715 A JPS59118715 A JP S59118715A
- Authority
- JP
- Japan
- Prior art keywords
- recovery rate
- purification
- solution
- substance
- buffer
- 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 42
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 42
- 230000003327 cancerostatic effect Effects 0.000 title abstract 2
- 238000000034 method Methods 0.000 claims abstract description 92
- 239000000126 substance Substances 0.000 claims abstract description 59
- 239000000243 solution Substances 0.000 claims abstract description 37
- 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 22
- 239000002158 endotoxin Substances 0.000 claims abstract description 19
- 238000006243 chemical reaction Methods 0.000 claims abstract description 12
- 108090001090 Lectins Proteins 0.000 claims abstract description 9
- 102000004856 Lectins Human genes 0.000 claims abstract description 9
- 239000002523 lectin Substances 0.000 claims abstract description 9
- 241000124008 Mammalia Species 0.000 claims abstract description 7
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 claims abstract description 6
- 241000894006 Bacteria Species 0.000 claims abstract description 6
- 230000000259 anti-tumor effect Effects 0.000 claims abstract description 6
- 238000010521 absorption reaction Methods 0.000 claims abstract description 5
- 150000001413 amino acids Chemical class 0.000 claims abstract description 3
- 239000007864 aqueous solution Substances 0.000 claims abstract description 3
- 238000000338 in vitro Methods 0.000 claims abstract description 3
- 238000001727 in vivo Methods 0.000 claims abstract description 3
- 230000002378 acidificating effect Effects 0.000 claims abstract 2
- 239000000872 buffer Substances 0.000 claims description 51
- 239000002244 precipitate Substances 0.000 claims description 20
- 230000001472 cytotoxic effect Effects 0.000 claims description 12
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 10
- 241000699670 Mus sp. Species 0.000 claims description 10
- 206010028980 Neoplasm Diseases 0.000 claims description 10
- 231100000433 cytotoxic Toxicity 0.000 claims description 10
- 230000003308 immunostimulating effect Effects 0.000 claims description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 4
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 4
- 238000005903 acid hydrolysis reaction Methods 0.000 claims description 2
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 claims description 2
- 241000282693 Cercopithecidae Species 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 109
- 239000007853 buffer solution Substances 0.000 abstract description 18
- 239000000463 material Substances 0.000 abstract description 8
- 238000001556 precipitation Methods 0.000 abstract description 3
- 206010039491 Sarcoma Diseases 0.000 abstract description 2
- OHJMTUPIZMNBFR-UHFFFAOYSA-N biuret Chemical compound NC(=O)NC(N)=O OHJMTUPIZMNBFR-UHFFFAOYSA-N 0.000 abstract description 2
- 239000003795 chemical substances by application Substances 0.000 abstract description 2
- 230000003013 cytotoxicity Effects 0.000 abstract description 2
- 231100000135 cytotoxicity Toxicity 0.000 abstract description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 abstract 2
- 239000011780 sodium chloride Substances 0.000 abstract 1
- 235000013311 vegetables Nutrition 0.000 abstract 1
- 238000011084 recovery Methods 0.000 description 84
- 238000000746 purification Methods 0.000 description 76
- 238000000108 ultra-filtration Methods 0.000 description 40
- 210000004027 cell Anatomy 0.000 description 37
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 34
- 238000000502 dialysis Methods 0.000 description 26
- 239000008363 phosphate buffer Substances 0.000 description 26
- 210000002966 serum Anatomy 0.000 description 26
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 25
- 235000011130 ammonium sulphate Nutrition 0.000 description 25
- 238000002523 gelfiltration Methods 0.000 description 23
- 210000004369 blood Anatomy 0.000 description 16
- 239000008280 blood Substances 0.000 description 16
- 238000010828 elution Methods 0.000 description 14
- 238000005406 washing Methods 0.000 description 12
- 241000283973 Oryctolagus cuniculus Species 0.000 description 11
- 238000005119 centrifugation Methods 0.000 description 11
- 210000003462 vein Anatomy 0.000 description 11
- 239000012141 concentrate Substances 0.000 description 10
- 239000000523 sample Substances 0.000 description 10
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 9
- 239000013543 active substance Substances 0.000 description 9
- 239000004202 carbamide Substances 0.000 description 9
- 238000001914 filtration Methods 0.000 description 9
- 230000001766 physiological effect Effects 0.000 description 9
- 239000000725 suspension Substances 0.000 description 9
- 238000005194 fractionation Methods 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 239000011734 sodium Substances 0.000 description 8
- 239000001488 sodium phosphate Substances 0.000 description 8
- 229910000162 sodium phosphate Inorganic materials 0.000 description 8
- 239000006228 supernatant Substances 0.000 description 8
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 8
- 108010052832 Cytochromes Proteins 0.000 description 7
- 102000018832 Cytochromes Human genes 0.000 description 7
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
- 201000011510 cancer Diseases 0.000 description 7
- 238000001962 electrophoresis Methods 0.000 description 7
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 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 description 7
- 238000005185 salting out 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
- 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 6
- 238000012360 testing method Methods 0.000 description 6
- 230000022534 cell killing Effects 0.000 description 5
- 230000003247 decreasing effect Effects 0.000 description 5
- 239000000385 dialysis solution Substances 0.000 description 5
- 229920006008 lipopolysaccharide Polymers 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 4
- 206010028851 Necrosis Diseases 0.000 description 4
- 102100040247 Tumor necrosis factor Human genes 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 239000002198 insoluble material Substances 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 201000001441 melanoma Diseases 0.000 description 4
- 230000017074 necrotic cell death Effects 0.000 description 4
- 208000020154 Acnes Diseases 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 229910019142 PO4 Inorganic materials 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
- 208000005718 Stomach Neoplasms Diseases 0.000 description 3
- 230000001093 anti-cancer Effects 0.000 description 3
- 239000002246 antineoplastic agent Substances 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 239000001569 carbon dioxide Substances 0.000 description 3
- 229910002092 carbon dioxide Inorganic materials 0.000 description 3
- 238000001816 cooling Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 238000004090 dissolution Methods 0.000 description 3
- 206010017758 gastric cancer Diseases 0.000 description 3
- 230000002008 hemorrhagic effect Effects 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 229940049954 penicillin Drugs 0.000 description 3
- 230000000144 pharmacologic effect Effects 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 201000011549 stomach cancer Diseases 0.000 description 3
- 229960005322 streptomycin Drugs 0.000 description 3
- 210000001179 synovial fluid Anatomy 0.000 description 3
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 208000011691 Burkitt lymphomas Diseases 0.000 description 2
- 108010038061 Chymotrypsinogen Proteins 0.000 description 2
- 108010062580 Concanavalin A Proteins 0.000 description 2
- 241000186427 Cutibacterium acnes Species 0.000 description 2
- 241001464975 Cutibacterium granulosum Species 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- 241000186359 Mycobacterium Species 0.000 description 2
- 241000283977 Oryctolagus Species 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 101710117064 Trimethylamine corrinoid protein 1 Proteins 0.000 description 2
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 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
- 239000006285 cell suspension Substances 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000012045 crude solution Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 238000011067 equilibration Methods 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
- 238000000691 measurement method Methods 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 108010001062 polysaccharide-K Proteins 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 229940055019 propionibacterium acne Drugs 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 108010048090 soybean lectin Proteins 0.000 description 2
- 239000003760 tallow Substances 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- 210000004885 white matter Anatomy 0.000 description 2
- 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 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-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
- 241000700198 Cavia Species 0.000 description 1
- -1 ConA) Proteins 0.000 description 1
- 108010007494 Cytochromes c6 Proteins 0.000 description 1
- 239000006145 Eagle's minimal essential medium Substances 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 1
- 241000186781 Listeria Species 0.000 description 1
- 101710085938 Matrix protein Proteins 0.000 description 1
- 101710127721 Membrane protein Proteins 0.000 description 1
- UEZVMMHDMIWARA-UHFFFAOYSA-N Metaphosphoric acid Chemical compound OP(=O)=O UEZVMMHDMIWARA-UHFFFAOYSA-N 0.000 description 1
- 208000002454 Nasopharyngeal Carcinoma Diseases 0.000 description 1
- 206010061306 Nasopharyngeal cancer Diseases 0.000 description 1
- 241000187678 Nocardia asteroides Species 0.000 description 1
- 108010058846 Ovalbumin Proteins 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
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 241000186429 Propionibacterium Species 0.000 description 1
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 241000293871 Salmonella enterica subsp. enterica serovar Typhi Species 0.000 description 1
- 208000003252 Signet Ring Cell Carcinoma Diseases 0.000 description 1
- 241000194017 Streptococcus Species 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
- YVNQAIFQFWTPLQ-UHFFFAOYSA-O [4-[[4-(4-ethoxyanilino)phenyl]-[4-[ethyl-[(3-sulfophenyl)methyl]amino]-2-methylphenyl]methylidene]-3-methylcyclohexa-2,5-dien-1-ylidene]-ethyl-[(3-sulfophenyl)methyl]azanium Chemical compound C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C(=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=2C(=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=C1 YVNQAIFQFWTPLQ-UHFFFAOYSA-O 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
- 239000002253 acid Substances 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 238000001467 acupuncture Methods 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229940088623 biologically active substance Drugs 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 230000005880 cancer cell killing Effects 0.000 description 1
- 208000025188 carcinoma of pharynx Diseases 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 108010018850 cytochrome C(551) Proteins 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
- 238000003370 dye binding method Methods 0.000 description 1
- 239000000839 emulsion Substances 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
- 238000009472 formulation Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 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
- PZLXYMQOCNYUIO-UHFFFAOYSA-N lithium;hydrochloride Chemical compound [Li].Cl PZLXYMQOCNYUIO-UHFFFAOYSA-N 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 1
- 201000011216 nasopharynx carcinoma Diseases 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 229910000498 pewter Inorganic materials 0.000 description 1
- 239000010957 pewter Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 238000011197 physicochemical method Methods 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 208000018655 severe necrosis Diseases 0.000 description 1
- 201000008123 signet ring cell adenocarcinoma Diseases 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57233949A JPS59118715A (ja) | 1982-12-24 | 1982-12-24 | 制ガン作用を有する低分子蛋白質 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57233949A JPS59118715A (ja) | 1982-12-24 | 1982-12-24 | 制ガン作用を有する低分子蛋白質 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS59118715A true JPS59118715A (ja) | 1984-07-09 |
| JPH0251440B2 JPH0251440B2 (enrdf_load_stackoverflow) | 1990-11-07 |
Family
ID=16963140
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP57233949A Granted JPS59118715A (ja) | 1982-12-24 | 1982-12-24 | 制ガン作用を有する低分子蛋白質 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS59118715A (enrdf_load_stackoverflow) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002211551A (ja) * | 2001-01-15 | 2002-07-31 | Dainippon Printing Co Ltd | 身蓋カートン |
| JP2007137495A (ja) * | 2005-11-21 | 2007-06-07 | Yanai Shiko Kk | 備品収納部付組立て紙蓋 |
-
1982
- 1982-12-24 JP JP57233949A patent/JPS59118715A/ja active Granted
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002211551A (ja) * | 2001-01-15 | 2002-07-31 | Dainippon Printing Co Ltd | 身蓋カートン |
| JP2007137495A (ja) * | 2005-11-21 | 2007-06-07 | Yanai Shiko Kk | 備品収納部付組立て紙蓋 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0251440B2 (enrdf_load_stackoverflow) | 1990-11-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JPS6030291B2 (ja) | 人顆粒球の分化増殖を促進するｈｇｉ糖蛋白質、ｈｇｉ糖蛋白質の製造法及びｈｇｉ糖蛋白質を含有する白血球減少症治療剤 | |
| US4845078A (en) | Method for treating hematopoietic diseases | |
| EP0132125B1 (en) | A protein having antitumor activity | |
| SU1012786A3 (ru) | Способ получени протеинового комплекса,стимулирующего секрецию инсулина | |
| JPH0539305A (ja) | アストラガルス・メンブラナセウスから抽出した免疫 変調性多糖類及びこれらを含有する薬剤組成物 | |
| JPH06507077A (ja) | 細菌高分子の抽出物、その調製のための方法及び前記抽出物を含む製薬組成物 | |
| JPS59118715A (ja) | 制ガン作用を有する低分子蛋白質 | |
| EP0246861B1 (en) | Use of compositions based on crotoxine, for the manufacture of a medicament for the treatment of carcinomas | |
| JPS59141519A (ja) | 制ガン作用を有する蛋白質 | |
| JPH0611705B2 (ja) | 血小板減少症治療剤 | |
| JPS608226A (ja) | 低分子蛋白質を有効成分とする制ガン剤 | |
| JPS59118714A (ja) | 制ガン作用を有する低分子蛋白質 | |
| JPS59118716A (ja) | 制ガン作用を有する低分子蛋白質 | |
| 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 | |
| JPS6226226A (ja) | 抗腫瘍性ポリペプチド | |
| JPS60243018A (ja) | ヒト内来性癌制御因子 | |
| JPS62258324A (ja) | 制ガン作用を有する糖蛋白質 | |
| JPS60226816A (ja) | 抗腫瘍活性をもつヒト由来蛋白質 | |
| JPH0566960B2 (enrdf_load_stackoverflow) | ||
| JPS62190128A (ja) | 腫瘍細胞増殖抑制および殺腫瘍細胞因子の製造法 | |
| JPS6137730A (ja) | 制ガン作用を有する蛋白質 | |
| KR19990025935A (ko) | 룸부로키나제의 제조방법과 이를 구성요소로 하는 액상제재및 용도 | |
| JPH0291100A (ja) | ヒトホスホリパーゼａ↓２阻害蛋白 | |
| JPS63215700A (ja) | 低分子量蛋白質 | |
| JPS6363559B2 (enrdf_load_stackoverflow) |