JPH0151997B2 - - Google Patents
Info
- Publication number
- JPH0151997B2 JPH0151997B2 JP55083920A JP8392080A JPH0151997B2 JP H0151997 B2 JPH0151997 B2 JP H0151997B2 JP 55083920 A JP55083920 A JP 55083920A JP 8392080 A JP8392080 A JP 8392080A JP H0151997 B2 JPH0151997 B2 JP H0151997B2
- Authority
- JP
- Japan
- Prior art keywords
- sodase
- blood cells
- copper
- red blood
- heating
- 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
- 102000004169 proteins and genes Human genes 0.000 claims description 33
- 108090000623 proteins and genes Proteins 0.000 claims description 33
- 210000003743 erythrocyte Anatomy 0.000 claims description 23
- 238000010438 heat treatment Methods 0.000 claims description 21
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 claims description 18
- 239000010949 copper Substances 0.000 claims description 18
- 238000000034 method Methods 0.000 claims description 18
- 229910052802 copper Inorganic materials 0.000 claims description 17
- 239000010941 cobalt Substances 0.000 claims description 16
- GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 claims description 16
- -1 alkali metal salt Chemical class 0.000 claims description 15
- 229910017052 cobalt Inorganic materials 0.000 claims description 15
- 239000006228 supernatant Substances 0.000 claims description 15
- 239000007788 liquid Substances 0.000 claims description 13
- 239000002244 precipitate Substances 0.000 claims description 12
- 229910052783 alkali metal Inorganic materials 0.000 claims description 10
- 150000002696 manganese Chemical class 0.000 claims description 10
- 150000003839 salts Chemical class 0.000 claims description 5
- 229910052748 manganese Inorganic materials 0.000 claims description 4
- 239000011572 manganese Substances 0.000 claims description 4
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 claims description 3
- 102000019197 Superoxide Dismutase Human genes 0.000 claims description 3
- 108010012715 Superoxide dismutase Proteins 0.000 claims description 3
- 230000001376 precipitating effect Effects 0.000 claims description 2
- ORTQZVOHEJQUHG-UHFFFAOYSA-L copper(II) chloride Chemical compound Cl[Cu]Cl ORTQZVOHEJQUHG-UHFFFAOYSA-L 0.000 description 26
- 102000001554 Hemoglobins Human genes 0.000 description 13
- 108010054147 Hemoglobins Proteins 0.000 description 13
- 210000000601 blood cell Anatomy 0.000 description 13
- 239000002994 raw material Substances 0.000 description 13
- 229960003280 cupric chloride Drugs 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 238000004925 denaturation Methods 0.000 description 6
- 230000036425 denaturation Effects 0.000 description 6
- 241000283690 Bos taurus Species 0.000 description 5
- 238000001816 cooling Methods 0.000 description 5
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 230000000052 comparative effect Effects 0.000 description 4
- 108010070915 orgotein Proteins 0.000 description 4
- 229960004534 orgotein Drugs 0.000 description 4
- 238000001556 precipitation Methods 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- JHJLBTNAGRQEKS-UHFFFAOYSA-M sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- TUGDLVFMIQZYPA-UHFFFAOYSA-N tetracopper;tetrazinc Chemical compound [Cu+2].[Cu+2].[Cu+2].[Cu+2].[Zn+2].[Zn+2].[Zn+2].[Zn+2] TUGDLVFMIQZYPA-UHFFFAOYSA-N 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000007853 buffer solution Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 150000001879 copper Chemical class 0.000 description 3
- 239000008367 deionised water Substances 0.000 description 3
- 229910021641 deionized water Inorganic materials 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 150000004045 organic chlorine compounds Chemical class 0.000 description 3
- 229910052723 transition metal Inorganic materials 0.000 description 3
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical group [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 2
- 239000003146 anticoagulant agent Substances 0.000 description 2
- 229940127219 anticoagulant drug Drugs 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- AMXOYNBUYSYVKV-UHFFFAOYSA-M lithium bromide Chemical compound [Li+].[Br-] AMXOYNBUYSYVKV-UHFFFAOYSA-M 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- IIPYXGDZVMZOAP-UHFFFAOYSA-N lithium nitrate Chemical compound [Li+].[O-][N+]([O-])=O IIPYXGDZVMZOAP-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 description 2
- 239000001103 potassium chloride Substances 0.000 description 2
- 235000011164 potassium chloride Nutrition 0.000 description 2
- FGIUAXJPYTZDNR-UHFFFAOYSA-N potassium nitrate Chemical compound [K+].[O-][N+]([O-])=O FGIUAXJPYTZDNR-UHFFFAOYSA-N 0.000 description 2
- VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Chemical compound [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 229910001429 cobalt ion Inorganic materials 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 229910001431 copper ion Inorganic materials 0.000 description 1
- XTVVROIMIGLXTD-UHFFFAOYSA-N copper(II) nitrate Chemical compound [Cu+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O XTVVROIMIGLXTD-UHFFFAOYSA-N 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 238000007323 disproportionation reaction Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 229910001437 manganese ion Inorganic materials 0.000 description 1
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 235000010333 potassium nitrate Nutrition 0.000 description 1
- 239000004323 potassium nitrate Substances 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 238000011403 purification operation Methods 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 235000011121 sodium hydroxide Nutrition 0.000 description 1
- 235000010344 sodium nitrate Nutrition 0.000 description 1
- 239000004317 sodium nitrate Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000011232 storage material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
Classifications
-
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0089—Oxidoreductases (1.) acting on superoxide as acceptor (1.15)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
- Y10S435/816—Enzyme separation or purification by solubility
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/829—Blood
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Description
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Claims (1)
- ïŒ èµ€è¡çã®æº¶è¡æ¶²ããå ç±ã«ããäžèŠèçœãæ²
柱é€å»ããŠãã¹ãŒããŒãªãã·ããžã¹ã ã¿ãŒãŒ
ïŒSuperoxide DismutaseïŒãåé¢ããæ¹æ³ã«ã
ããŠãèµ€è¡ç溶è¡æ¶²ãã¢ã«ã«ãªéå±ã®å¡©ããã³
é ãã³ãã«ãããŸãã¯ãã³ã¬ã³ã®å¡©ã®ååšäžã«å
ç±ããŠçããæ²æŸ±ãé€å»ãã第ïŒå·¥çšãšããã®äž
æŸæ¶²ã«ç¬¬ïŒå·¥çšãšåé以äžã®é ãã³ãã«ãããŸã
ã¯ãã³ã¬ã³ã®å¡©ãæ·»å ããå ç±ããŠçããæ²æŸ±ã
é€å»ãã第ïŒå·¥çšãšããçµã¿åããããšãç¹åŸŽãš
ããã¹ãŒããŒãªãã·ããžã¹ã ã¿ãŒãŒã®åé¢æ¹æ³ã
Priority Applications (6)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP8392080A JPS5712993A (en) | 1980-06-23 | 1980-06-23 | Isolation of superoxide dismutase |
US06/275,392 US4346174A (en) | 1980-06-23 | 1981-06-19 | Process for isolating superoxide dismutase from red blood cells |
DE3124228A DE3124228C2 (de) | 1980-06-23 | 1981-06-20 | Verfahren zur Isolierung von Superoxid-dismutase aus roten Blutzellen |
NL8102998A NL8102998A (nl) | 1980-06-23 | 1981-06-22 | Werkwijze voor het isoleren van superoxide-dismutase uit rode bloedcellen. |
GB8119195A GB2081273B (en) | 1980-06-23 | 1981-06-22 | Process for isolating superoxide dismutase from red blood cells |
FR8112286A FR2485203A1 (fr) | 1980-06-23 | 1981-06-23 | Procede pour isoler la dismutase peroxydee des hematies |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP8392080A JPS5712993A (en) | 1980-06-23 | 1980-06-23 | Isolation of superoxide dismutase |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS5712993A JPS5712993A (en) | 1982-01-22 |
JPH0151997B2 true JPH0151997B2 (ja) | 1989-11-07 |
Family
ID=13816032
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP8392080A Granted JPS5712993A (en) | 1980-06-23 | 1980-06-23 | Isolation of superoxide dismutase |
Country Status (6)
Country | Link |
---|---|
US (1) | US4346174A (ja) |
JP (1) | JPS5712993A (ja) |
DE (1) | DE3124228C2 (ja) |
FR (1) | FR2485203A1 (ja) |
GB (1) | GB2081273B (ja) |
NL (1) | NL8102998A (ja) |
Families Citing this family (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5714362A (en) * | 1983-04-29 | 1998-02-03 | Yeda Research And Development Co. Ltd. | Human superoxide dismutase cDNA |
DE3486493T2 (de) * | 1983-10-03 | 2003-05-22 | Chiron Corp. (N.D.Ges.D. Staates Delaware), Emeryville | Klonieren von Superoxiddismutase und Expression in Mikroorganismen |
US4585754A (en) * | 1984-01-09 | 1986-04-29 | Valcor Scientific, Ltd. | Stabilization of proteins and peptides by chemical binding with chondroitin |
DE3410159A1 (de) * | 1984-03-20 | 1985-09-26 | Alfred Dipl.-Biochem. 7400 TÌbingen GÀrtner | Verfahren zur gewinnung von cu(pfeil abwaerts)2(pfeil abwaerts)zn(pfeil abwaerts)2(pfeil abwaerts)superoxiddismutase aus roten blutzellen von wirbeltieren |
US5162217A (en) * | 1984-08-27 | 1992-11-10 | Bio-Technology General Corp. | Plasmids for expression of human superoxide dismutase (SOD) analogs containing lambda PL promoter with engineered restriction site for substituting ribosomal binding sites and methods of use thereof |
US6030611A (en) * | 1984-08-27 | 2000-02-29 | Bio-Technology General Corp. | Therapeutic SOD compositions and uses thereof |
US4940659A (en) * | 1987-02-20 | 1990-07-10 | Monoclonetics International, Inc. | Screening extra-cellular body fluids for superoxide dismutase (SOD-1) for determining fetal trisomy 21 down syndrome |
US5227405A (en) * | 1987-03-31 | 1993-07-13 | Duke University | Superoxide dismutase mimic |
US5223538A (en) * | 1987-03-31 | 1993-06-29 | Duke University | Superoxide dismutase mimic |
DE4239877C1 (de) * | 1992-11-27 | 1994-03-17 | Boehringer Ingelheim Int | Stabilisierte Superoxid-Dismutase (SOD)-Zusammensetzung |
US5486360A (en) * | 1993-04-22 | 1996-01-23 | St. Joseph Health Centre | Method of treating tumour cells using catalase |
Family Cites Families (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IL32097A (en) * | 1968-05-13 | 1973-08-29 | Diagnostic Data Inc | Isolation of orgotein from blood |
CA924640A (en) * | 1970-01-16 | 1973-04-17 | Huber Wolfgang | Orgotein purification process |
US3624251A (en) * | 1970-01-16 | 1971-11-30 | Diagnostic Data Inc | Orgotein purification process by heating above 65{20 {0 c. |
US3579495A (en) * | 1970-04-24 | 1971-05-18 | Diagnostic Data Inc | Isolation of orgotein from blood |
US3687927A (en) * | 1971-06-07 | 1972-08-29 | Diagnostic Data Inc | Orgotein isolation process employing single ion exchange resin having both acidic and basic groups |
US3763137A (en) * | 1971-12-07 | 1973-10-02 | Diagnostic Data Inc | Isolation of orgotein from red blood cells |
US3832338A (en) * | 1972-03-23 | 1974-08-27 | Diagnostic Data Inc | Orgotein production using a buffer solution containing divalent metal salts |
US3813289A (en) * | 1972-07-19 | 1974-05-28 | Diagnostic Data Inc | Orgotein from red blood cells |
IL40955A (en) * | 1972-07-19 | 1975-11-25 | Diagnostic Data Inc | The production of orgotein from red blood cells |
-
1980
- 1980-06-23 JP JP8392080A patent/JPS5712993A/ja active Granted
-
1981
- 1981-06-19 US US06/275,392 patent/US4346174A/en not_active Expired - Fee Related
- 1981-06-20 DE DE3124228A patent/DE3124228C2/de not_active Expired
- 1981-06-22 GB GB8119195A patent/GB2081273B/en not_active Expired
- 1981-06-22 NL NL8102998A patent/NL8102998A/nl not_active Application Discontinuation
- 1981-06-23 FR FR8112286A patent/FR2485203A1/fr active Granted
Also Published As
Publication number | Publication date |
---|---|
GB2081273B (en) | 1983-06-29 |
DE3124228C2 (de) | 1986-09-25 |
US4346174A (en) | 1982-08-24 |
NL8102998A (nl) | 1982-01-18 |
GB2081273A (en) | 1982-02-17 |
JPS5712993A (en) | 1982-01-22 |
DE3124228A1 (de) | 1982-02-25 |
FR2485203A1 (fr) | 1981-12-24 |
FR2485203B1 (ja) | 1984-04-06 |
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