DD208988A5 - Verfahren zum aufbau eines chimaeren plasmids mit einer genkodierung fuer eine thermostabile alpha-amylase - Google Patents
Verfahren zum aufbau eines chimaeren plasmids mit einer genkodierung fuer eine thermostabile alpha-amylase Download PDFInfo
- Publication number
- DD208988A5 DD208988A5 DD82236740A DD23674082A DD208988A5 DD 208988 A5 DD208988 A5 DD 208988A5 DD 82236740 A DD82236740 A DD 82236740A DD 23674082 A DD23674082 A DD 23674082A DD 208988 A5 DD208988 A5 DD 208988A5
- Authority
- DD
- German Democratic Republic
- Prior art keywords
- amylase
- plasmid
- alpha
- cells
- gene
- Prior art date
Links
- 108090000637 alpha-Amylases Proteins 0.000 title claims abstract description 58
- 238000000034 method Methods 0.000 title claims abstract description 49
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 47
- 102000004139 alpha-Amylases Human genes 0.000 title claims abstract description 46
- 229940024171 alpha-amylase Drugs 0.000 title claims abstract description 36
- 239000013612 plasmid Substances 0.000 claims abstract description 122
- 244000005700 microbiome Species 0.000 claims abstract description 34
- 108010065511 Amylases Proteins 0.000 claims description 48
- 102000013142 Amylases Human genes 0.000 claims description 37
- 235000019418 amylase Nutrition 0.000 claims description 36
- 239000004382 Amylase Substances 0.000 claims description 33
- 239000013598 vector Substances 0.000 claims description 25
- 241000588724 Escherichia coli Species 0.000 claims description 12
- 239000012634 fragment Substances 0.000 claims description 12
- 108091008146 restriction endonucleases Proteins 0.000 claims description 10
- 101000588924 Anthopleura elegantissima Delta-actitoxin-Ael1a Proteins 0.000 claims description 9
- 101150101441 dus gene Proteins 0.000 claims description 7
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 5
- 102000003960 Ligases Human genes 0.000 claims description 5
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- 238000003776 cleavage reaction Methods 0.000 claims description 3
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- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 11
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- 239000003550 marker Substances 0.000 description 6
- 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 5
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- 150000003522 tetracyclines Chemical class 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 108010042407 Endonucleases Proteins 0.000 description 4
- 102000004533 Endonucleases Human genes 0.000 description 4
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 4
- 229930006000 Sucrose Natural products 0.000 description 4
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 4
- 238000005520 cutting process Methods 0.000 description 4
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- 238000012360 testing method Methods 0.000 description 4
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- 229940025131 amylases Drugs 0.000 description 3
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- 229920002261 Corn starch Polymers 0.000 description 2
- DYDCUQKUCUHJBH-UWTATZPHSA-N D-Cycloserine Chemical compound N[C@@H]1CONC1=O DYDCUQKUCUHJBH-UWTATZPHSA-N 0.000 description 2
- DYDCUQKUCUHJBH-UHFFFAOYSA-N D-Cycloserine Natural products NC1CONC1=O DYDCUQKUCUHJBH-UHFFFAOYSA-N 0.000 description 2
- 230000004544 DNA amplification Effects 0.000 description 2
- 244000025221 Humulus lupulus Species 0.000 description 2
- 235000008694 Humulus lupulus Nutrition 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
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- 239000007478 blood agar base Substances 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
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- 230000002934 lysing effect Effects 0.000 description 2
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- 238000003786 synthesis reaction Methods 0.000 description 2
- 241000304886 Bacilli Species 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102100031920 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial Human genes 0.000 description 1
- 101000992065 Homo sapiens Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
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- 102000029797 Prion Human genes 0.000 description 1
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- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
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- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
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- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
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- 230000003321 amplification Effects 0.000 description 1
- 206010002022 amyloidosis Diseases 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
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- 239000000872 buffer Substances 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- XLJKHNWPARRRJB-UHFFFAOYSA-N cobalt(2+) Chemical compound [Co+2] XLJKHNWPARRRJB-UHFFFAOYSA-N 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000002285 corn oil Substances 0.000 description 1
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- 238000001773 deep-level transient spectroscopy Methods 0.000 description 1
- 238000002298 density-gradient ultracentrifugation Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- IWEDIXLBFLAXBO-UHFFFAOYSA-N dicamba Chemical compound COC1=C(Cl)C=CC(Cl)=C1C(O)=O IWEDIXLBFLAXBO-UHFFFAOYSA-N 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
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- 235000019319 peptone Nutrition 0.000 description 1
- 239000000575 pesticide Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 239000000583 progesterone congener Substances 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 235000011888 snacks Nutrition 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 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
- 210000002325 somatostatin-secreting cell Anatomy 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
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- 229930003231 vitamin Natural products 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
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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
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Medicinal Preparation (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Dental Preparations (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US22528781A | 1981-01-15 | 1981-01-15 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DD208988A5 true DD208988A5 (de) | 1984-04-18 |
Family
ID=22844306
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DD82236740A DD208988A5 (de) | 1981-01-15 | 1982-01-14 | Verfahren zum aufbau eines chimaeren plasmids mit einer genkodierung fuer eine thermostabile alpha-amylase |
Country Status (16)
| Country | Link |
|---|---|
| EP (1) | EP0057976B1 (fr) |
| JP (1) | JPS57139097A (fr) |
| AT (1) | ATE17373T1 (fr) |
| CA (1) | CA1170202A (fr) |
| DD (1) | DD208988A5 (fr) |
| DE (1) | DE3268340D1 (fr) |
| DK (1) | DK157879C (fr) |
| ES (2) | ES8305041A1 (fr) |
| FI (1) | FI79139C (fr) |
| HU (1) | HU193516B (fr) |
| IE (1) | IE52434B1 (fr) |
| IL (1) | IL64741A (fr) |
| MX (1) | MX7066E (fr) |
| SU (1) | SU1200853A3 (fr) |
| YU (2) | YU9682A (fr) |
| ZA (1) | ZA82133B (fr) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4886754A (en) * | 1980-01-07 | 1989-12-12 | The University Of Rochester | Recombinant bateriophage for heterologous cloning of bacillus microorganisms and method for its production |
| FR2533583A1 (fr) * | 1982-09-24 | 1984-03-30 | Centre Nat Rech Scient | Nouvel adn recombinant utile dans la preparation d'a-amylase |
| ATE48156T1 (de) * | 1982-11-01 | 1989-12-15 | Miles Inc | Verfahren zur heterologen klonierung eines gens in einem bacillus-mikroorganismus. |
| US4559300A (en) * | 1983-01-18 | 1985-12-17 | Eli Lilly And Company | Method for using an homologous bacillus promoter and associated natural or modified ribosome binding site-containing DNA sequence in streptomyces |
| JPS59196092A (ja) * | 1983-04-25 | 1984-11-07 | Sanraku Inc | 組換えプラスミドによる耐熱性α−アミラ−ゼの新規製造法 |
| NZ208612A (en) * | 1983-06-24 | 1991-09-25 | Genentech Inc | Method of producing "procaryotic carbonyl hydrolases" containing predetermined, site specific mutations |
| AU587960B2 (en) * | 1983-06-24 | 1989-09-07 | Genentech Inc. | Procaryotic carbonyl hydrolases |
| US4578352A (en) * | 1983-07-13 | 1986-03-25 | Cpc International Inc. | Novel thermostable, aciduric alpha-amylase and method for its production |
| GB8333797D0 (en) * | 1983-12-19 | 1984-01-25 | Searle & Co | Starch utilization |
| US5032510A (en) * | 1984-09-26 | 1991-07-16 | Eli Lilly And Company | Method for expression and secretion in bacillus |
| WO1986005812A1 (fr) * | 1985-03-29 | 1986-10-09 | Biotechnica International, Inc. | Vecteur de secretion |
| JPH0616711B2 (ja) * | 1985-09-27 | 1994-03-09 | メルシャン株式会社 | 高温で自律増殖するプラスミド |
| US5278059A (en) * | 1985-12-04 | 1994-01-11 | Kabushiki Kaisha Hayashibara Seibutsu Kagaki Kenkyujo | Polypeptide possessing cyclomaltodextrin glucanotransferase activity |
| IN165610B (fr) * | 1986-12-22 | 1989-11-25 | Enzyme Bio Systems Ltd | |
| US4977089A (en) * | 1987-01-30 | 1990-12-11 | Eli Lilly And Company | Vector comprising signal peptide-encoding DNA for use in Bacillus and other microorganisms |
| WO1991000353A2 (fr) * | 1989-06-29 | 1991-01-10 | Gist-Brocades N.V. | α-AMYLASES MICROBIENNES MUTANTES PRESENTANT UNE MEILLEURE STABILITE THERMIQUE, AUX ACIDES ET/OU AUX ALCALINS |
| NL8902128A (nl) * | 1989-08-23 | 1991-03-18 | Avebe Coop Verkoop Prod | Vertakkingsenzym en gebruik daarvan. |
| US6300115B1 (en) | 1998-05-18 | 2001-10-09 | Enzyme Bio-Systems Ltd. | Pullulanase expression constructs containing α-amylase promoter and leader sequences |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ183818A (en) * | 1976-04-19 | 1980-05-08 | Cpc International Inc | Heat -and acid-stable alpha-amylase and process for converting starch to a starch hydrolysate |
| IL61982A (en) * | 1980-02-15 | 1984-01-31 | Cpc International Inc | Genetically engineered microorganisms for massive production of amyloytic enzymes and process for preparing same using the corresponding recombinant dnas containing amylase coding genes |
-
1982
- 1982-01-08 CA CA000393781A patent/CA1170202A/fr not_active Expired
- 1982-01-08 IE IE32/82A patent/IE52434B1/en unknown
- 1982-01-08 ZA ZA82133A patent/ZA82133B/xx unknown
- 1982-01-10 IL IL64741A patent/IL64741A/xx unknown
- 1982-01-12 DE DE8282300158T patent/DE3268340D1/de not_active Expired
- 1982-01-12 AT AT82300158T patent/ATE17373T1/de not_active IP Right Cessation
- 1982-01-12 EP EP82300158A patent/EP0057976B1/fr not_active Expired
- 1982-01-13 ES ES508694A patent/ES8305041A1/es not_active Expired
- 1982-01-13 FI FI820107A patent/FI79139C/fi not_active IP Right Cessation
- 1982-01-14 DD DD82236740A patent/DD208988A5/de unknown
- 1982-01-14 JP JP57003522A patent/JPS57139097A/ja active Pending
- 1982-01-14 SU SU823383349A patent/SU1200853A3/ru active
- 1982-01-14 MX MX829870U patent/MX7066E/es unknown
- 1982-01-14 DK DK013182A patent/DK157879C/da active
- 1982-01-15 YU YU00096/82A patent/YU9682A/xx unknown
- 1982-01-15 HU HU82114A patent/HU193516B/hu not_active IP Right Cessation
- 1982-12-14 ES ES518157A patent/ES8405070A1/es not_active Expired
-
1984
- 1984-10-15 YU YU01763/84A patent/YU176384A/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| ES518157A0 (es) | 1984-05-16 |
| ES508694A0 (es) | 1983-03-16 |
| DE3268340D1 (en) | 1986-02-20 |
| IL64741A0 (en) | 1982-03-31 |
| FI79139C (fi) | 1989-11-10 |
| EP0057976B1 (fr) | 1986-01-08 |
| DK157879B (da) | 1990-02-26 |
| YU9682A (en) | 1985-06-30 |
| EP0057976A3 (en) | 1982-09-01 |
| YU176384A (en) | 1987-02-28 |
| ES8305041A1 (es) | 1983-03-16 |
| DK13182A (da) | 1982-07-16 |
| HU193516B (en) | 1987-10-28 |
| ZA82133B (en) | 1983-02-23 |
| SU1200853A3 (ru) | 1985-12-23 |
| FI820107L (fi) | 1982-07-16 |
| IL64741A (en) | 1985-07-31 |
| FI79139B (fi) | 1989-07-31 |
| IE52434B1 (en) | 1987-10-28 |
| JPS57139097A (en) | 1982-08-27 |
| IE820032L (en) | 1982-07-15 |
| CA1170202A (fr) | 1984-07-03 |
| DK157879C (da) | 1990-07-30 |
| ES8405070A1 (es) | 1984-05-16 |
| EP0057976A2 (fr) | 1982-08-18 |
| ATE17373T1 (de) | 1986-01-15 |
| MX7066E (es) | 1987-04-20 |
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