CA1295558C - Synthesis of long chain dna - Google Patents
Synthesis of long chain dnaInfo
- Publication number
- CA1295558C CA1295558C CA000498535A CA498535A CA1295558C CA 1295558 C CA1295558 C CA 1295558C CA 000498535 A CA000498535 A CA 000498535A CA 498535 A CA498535 A CA 498535A CA 1295558 C CA1295558 C CA 1295558C
- Authority
- CA
- Canada
- Prior art keywords
- dna
- long chain
- synthesis
- gene
- chain dna
- 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 - Lifetime
Links
- 230000015572 biosynthetic process Effects 0.000 title abstract description 13
- 238000003786 synthesis reaction Methods 0.000 title abstract description 13
- 238000000034 method Methods 0.000 claims abstract description 32
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 20
- 230000002194 synthesizing effect Effects 0.000 claims description 9
- 238000009833 condensation Methods 0.000 claims description 7
- 230000005494 condensation Effects 0.000 claims description 7
- 239000005289 controlled pore glass Substances 0.000 claims description 7
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 claims description 4
- 239000003795 chemical substances by application Substances 0.000 claims description 3
- -1 phosphate triester Chemical class 0.000 claims description 3
- 125000003277 amino group Chemical group 0.000 claims description 2
- 229910019142 PO4 Inorganic materials 0.000 claims 1
- 239000010452 phosphate Substances 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 abstract description 4
- 150000005691 triesters Chemical class 0.000 abstract description 3
- 239000007787 solid Substances 0.000 abstract description 2
- 108020004414 DNA Proteins 0.000 description 45
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 13
- 108010049140 Endorphins Proteins 0.000 description 12
- 125000002103 4,4'-dimethoxytriphenylmethyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)(C1=C([H])C([H])=C(OC([H])([H])[H])C([H])=C1[H])C1=C([H])C([H])=C(OC([H])([H])[H])C([H])=C1[H] 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical group C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 10
- 239000013612 plasmid Substances 0.000 description 10
- 102000053602 DNA Human genes 0.000 description 8
- 108020003215 DNA Probes Proteins 0.000 description 7
- 239000003298 DNA probe Substances 0.000 description 7
- 102000009025 Endorphins Human genes 0.000 description 7
- 108010041395 alpha-Endorphin Proteins 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 6
- 108090000765 processed proteins & peptides Proteins 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 239000012634 fragment Substances 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 5
- 102000012410 DNA Ligases Human genes 0.000 description 4
- 108010061982 DNA Ligases Proteins 0.000 description 4
- 102100038796 E3 ubiquitin-protein ligase TRIM13 Human genes 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 101000664589 Homo sapiens E3 ubiquitin-protein ligase TRIM13 Proteins 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 238000010532 solid phase synthesis reaction Methods 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- DNWBUCHHMRQWCZ-GUBZILKMSA-N Lys-Ser-Gln Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(N)=O DNWBUCHHMRQWCZ-GUBZILKMSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- DEGCBBCMYWNJNA-RHYQMDGZSA-N Thr-Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)[C@@H](C)O DEGCBBCMYWNJNA-RHYQMDGZSA-N 0.000 description 3
- XHWCDRUPDNSDAZ-XKBZYTNZSA-N Thr-Ser-Glu Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N)O XHWCDRUPDNSDAZ-XKBZYTNZSA-N 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- PVNNAAWVJPIJHS-CQJMVLFOSA-N (2s)-2-[[(2s)-2-[[2-[[2-[[(2s)-2-[[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylsulfanylbutanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](N)CCCN=C(N)N)C1=CC=CC=C1 PVNNAAWVJPIJHS-CQJMVLFOSA-N 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 108010022337 Leucine Enkephalin Proteins 0.000 description 2
- CULGJGUDIJATIP-STQMWFEESA-N Met-Tyr-Gly Chemical compound CSCC[C@H](N)C(=O)N[C@H](C(=O)NCC(O)=O)CC1=CC=C(O)C=C1 CULGJGUDIJATIP-STQMWFEESA-N 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- 102100029563 Somatostatin Human genes 0.000 description 2
- BQBCIBCLXBKYHW-CSMHCCOUSA-N Thr-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@@H]([NH3+])[C@@H](C)O BQBCIBCLXBKYHW-CSMHCCOUSA-N 0.000 description 2
- 238000000211 autoradiogram Methods 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 229940039227 diagnostic agent Drugs 0.000 description 2
- 239000000032 diagnostic agent Substances 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 108010047064 gamma-Endorphin Proteins 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 2
- 238000010647 peptide synthesis reaction Methods 0.000 description 2
- 239000000741 silica gel Substances 0.000 description 2
- 229910002027 silica gel Inorganic materials 0.000 description 2
- NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 2
- 229960000553 somatostatin Drugs 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- YCICLRBTJMLLGG-UHFFFAOYSA-N (2-chlorophenyl) dihydrogen phosphate Chemical compound OP(O)(=O)OC1=CC=CC=C1Cl YCICLRBTJMLLGG-UHFFFAOYSA-N 0.000 description 1
- RNHDAKUGFHSZEV-UHFFFAOYSA-N 1,4-dioxane;hydrate Chemical compound O.C1COCCO1 RNHDAKUGFHSZEV-UHFFFAOYSA-N 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 101800005049 Beta-endorphin Proteins 0.000 description 1
- 102400000748 Beta-endorphin Human genes 0.000 description 1
- 101100148606 Caenorhabditis elegans pst-1 gene Proteins 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 102400000113 Calcitonin Human genes 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 102400000921 Gastrin Human genes 0.000 description 1
- 108010052343 Gastrins Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 101000632994 Homo sapiens Somatostatin Proteins 0.000 description 1
- 208000037147 Hypercalcaemia Diseases 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- CFFXTXXQXWZQNT-UHFFFAOYSA-N N1=CC=CC=C1.CN(C(N(C)C)=N)C Chemical compound N1=CC=CC=C1.CN(C(N(C)C)=N)C CFFXTXXQXWZQNT-UHFFFAOYSA-N 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- ZYPUVVZACMVNBV-UHFFFAOYSA-N S(=O)(=O)=C1[CH-]N(N=N1)[N+](=O)[O-].C1(=CC(=CC(=C1)C)C)C Chemical compound S(=O)(=O)=C1[CH-]N(N=N1)[N+](=O)[O-].C1(=CC(=CC(=C1)C)C)C ZYPUVVZACMVNBV-UHFFFAOYSA-N 0.000 description 1
- 108010086019 Secretin Proteins 0.000 description 1
- 102100037505 Secretin Human genes 0.000 description 1
- 108010056088 Somatostatin Proteins 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- CIHUOJZDKZENCP-UHFFFAOYSA-N acetonitrile;triethylazanium;acetate Chemical compound CC#N.CC(O)=O.CCN(CC)CC CIHUOJZDKZENCP-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 235000011114 ammonium hydroxide Nutrition 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- SRSXLGNVWSONIS-UHFFFAOYSA-N benzenesulfonic acid Chemical compound OS(=O)(=O)C1=CC=CC=C1 SRSXLGNVWSONIS-UHFFFAOYSA-N 0.000 description 1
- 229940092714 benzenesulfonic acid Drugs 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- WOPZMFQRCBYPJU-NTXHZHDSSA-N beta-endorphin Chemical compound C([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)O)C1=CC=CC=C1 WOPZMFQRCBYPJU-NTXHZHDSSA-N 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 238000005266 casting Methods 0.000 description 1
- AOXOCDRNSPFDPE-UKEONUMOSA-N chembl413654 Chemical compound C([C@H](C(=O)NCC(=O)N[C@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@H](CCSC)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](C)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]1N(CCC1)C(=O)CNC(=O)[C@@H](N)CCC(O)=O)C1=CC=C(O)C=C1 AOXOCDRNSPFDPE-UKEONUMOSA-N 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000006482 condensation reaction Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006642 detritylation reaction Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 210000001198 duodenum Anatomy 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000002124 endocrine Effects 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000000148 hypercalcaemia Effects 0.000 description 1
- 208000030915 hypercalcemia disease Diseases 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229960005181 morphine Drugs 0.000 description 1
- PSHKMPUSSFXUIA-UHFFFAOYSA-N n,n-dimethylpyridin-2-amine Chemical compound CN(C)C1=CC=CC=N1 PSHKMPUSSFXUIA-UHFFFAOYSA-N 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- OENLEHTYJXMVBG-UHFFFAOYSA-N pyridine;hydrate Chemical compound [OH-].C1=CC=[NH+]C=C1 OENLEHTYJXMVBG-UHFFFAOYSA-N 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 229960002101 secretin Drugs 0.000 description 1
- OWMZNFCDEHGFEP-NFBCVYDUSA-N secretin human Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(N)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)C1=CC=CC=C1 OWMZNFCDEHGFEP-NFBCVYDUSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
- ONSIBMFFLJKTPT-UHFFFAOYSA-L zinc;2,3,4,5,6-pentachlorobenzenethiolate Chemical compound [Zn+2].[S-]C1=C(Cl)C(Cl)=C(Cl)C(Cl)=C1Cl.[S-]C1=C(Cl)C(Cl)=C(Cl)C(Cl)=C1Cl ONSIBMFFLJKTPT-UHFFFAOYSA-L 0.000 description 1
- NXSIJWJXMWBCBX-NWKQFZAZSA-N α-endorphin Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 NXSIJWJXMWBCBX-NWKQFZAZSA-N 0.000 description 1
- GASYAMBJHBRTOE-WHDBNHDESA-N γ-endorphin Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 GASYAMBJHBRTOE-WHDBNHDESA-N 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/665—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans derived from pro-opiomelanocortin, pro-enkephalin or pro-dynorphin
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Toxicology (AREA)
- Physics & Mathematics (AREA)
- Gastroenterology & Hepatology (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP59-281645 | 1984-12-26 | ||
JP59281645A JPS61152695A (ja) | 1984-12-26 | 1984-12-26 | 長鎖dnaの合成法 |
Publications (1)
Publication Number | Publication Date |
---|---|
CA1295558C true CA1295558C (en) | 1992-02-11 |
Family
ID=17641986
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA000498535A Expired - Lifetime CA1295558C (en) | 1984-12-26 | 1985-12-23 | Synthesis of long chain dna |
Country Status (9)
Country | Link |
---|---|
JP (1) | JPS61152695A (ko) |
KR (1) | KR940000543B1 (ko) |
CA (1) | CA1295558C (ko) |
CH (1) | CH672791A5 (ko) |
DE (1) | DE3544459C2 (ko) |
ES (1) | ES8802330A1 (ko) |
FR (1) | FR2575162B1 (ko) |
GB (1) | GB2169605B (ko) |
IT (1) | IT1208725B (ko) |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5114839A (en) * | 1988-05-24 | 1992-05-19 | Gesellschaft Fur Biotechnologische Forsching Mbh | Process for dna sequencing using oligonucleotide bank |
EP0638089B2 (en) * | 1992-04-15 | 2008-03-05 | The Johns Hopkins University | Synthesis of diverse and useful collections of oligonucleotides |
US5516664A (en) * | 1992-12-23 | 1996-05-14 | Hyman; Edward D. | Enzymatic synthesis of repeat regions of oligonucleotides |
US6479262B1 (en) | 2000-05-16 | 2002-11-12 | Hercules, Incorporated | Solid phase enzymatic assembly of polynucleotides |
US7205399B1 (en) | 2001-07-06 | 2007-04-17 | Sirna Therapeutics, Inc. | Methods and reagents for oligonucleotide synthesis |
Family Cites Families (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
BR7807288A (pt) * | 1977-11-08 | 1979-06-12 | Genentech Inc | Processo para sintese de polinucleotidos |
EP0173356B1 (en) * | 1980-02-29 | 1990-09-19 | University Patents, Inc. | Process for preparing modified inorganic polymers |
EP0102995A1 (en) * | 1982-03-08 | 1984-03-21 | Celltech Limited | Polynucleotide synthesis |
EP0090789A1 (en) * | 1982-03-26 | 1983-10-05 | Monsanto Company | Chemical DNA synthesis |
IL69196A0 (en) * | 1982-08-20 | 1983-11-30 | Genex Corp | Solid phase synthesis of oligonucleotides |
DE3301833A1 (de) * | 1983-01-20 | 1984-07-26 | Gesellschaft für Biotechnologische Forschung mbH (GBF), 3300 Braunschweig | Verfahren zur simultanen synthese mehrerer oligonocleotide an fester phase |
EP0155950B1 (en) * | 1983-09-02 | 1990-01-17 | Molecular Biosystems, Inc. | Oligonucleotide polymeric support system |
PT79519B (en) * | 1983-11-21 | 1986-12-11 | Ciba Geigy Ag | Process for preparing protease inhibitors based on egline compounds |
-
1984
- 1984-12-26 JP JP59281645A patent/JPS61152695A/ja active Granted
-
1985
- 1985-12-16 GB GB8530915A patent/GB2169605B/en not_active Expired
- 1985-12-16 DE DE3544459A patent/DE3544459C2/de not_active Expired - Fee Related
- 1985-12-18 IT IT8548954A patent/IT1208725B/it active
- 1985-12-20 FR FR858518965A patent/FR2575162B1/fr not_active Expired
- 1985-12-20 CH CH5457/85A patent/CH672791A5/fr not_active IP Right Cessation
- 1985-12-23 CA CA000498535A patent/CA1295558C/en not_active Expired - Lifetime
- 1985-12-24 ES ES550390A patent/ES8802330A1/es not_active Expired
- 1985-12-26 KR KR1019850009935A patent/KR940000543B1/ko active IP Right Grant
Also Published As
Publication number | Publication date |
---|---|
ES8802330A1 (es) | 1988-05-01 |
GB2169605B (en) | 1989-06-07 |
ES550390A0 (es) | 1988-05-01 |
IT8548954A0 (it) | 1985-12-18 |
FR2575162A1 (fr) | 1986-06-27 |
KR860005025A (ko) | 1986-07-16 |
KR940000543B1 (ko) | 1994-01-24 |
GB8530915D0 (en) | 1986-01-29 |
DE3544459C2 (de) | 1993-12-16 |
IT1208725B (it) | 1989-07-10 |
FR2575162B1 (fr) | 1989-05-05 |
GB2169605A (en) | 1986-07-16 |
JPS61152695A (ja) | 1986-07-11 |
DE3544459A1 (de) | 1986-07-03 |
JPH0586400B2 (ko) | 1993-12-10 |
CH672791A5 (ko) | 1989-12-29 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
DK175182B1 (da) | Mini-proinsulin, denne forbindelse til anvendelse som lægemiddel, lægemiddel indeholdende forbindelsen, anvendelse af forbindelsen til fremstilling af mono-Arg-insulin, fremgangsmåde til fremstilling af forbindelsen, DNA, der koder for forbindelsen...... | |
EP0238101A1 (en) | Microbial expression of interleukin II | |
NL192116C (nl) | Beta-urogastron-genen, overeenkomstige recombinant plasmiden, overeen- komstige transformanten en de bereiding ervan en van beta-urogastron. | |
US5149657A (en) | Escherichia coli expression vector encoding bioadhesive precursor protein analogs comprising three to twenty repeats of the decapeptide (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) | |
WO1983004030A1 (en) | The manufacture and expression of genes for urogastrone and polypeptide analogs thereof | |
JPS6012986A (ja) | 成熟ヒトil−2をコ−ドする2本鎖ポリデオキシリボヌクレオチド | |
CA1295558C (en) | Synthesis of long chain dna | |
JP6959251B2 (ja) | ナノポアシステムに有用な部位特異的バイオコンジュゲーション方法および組成物 | |
JPH05184381A (ja) | 組換えgrfの製造方法 | |
JPS6049798A (ja) | 酸アミド−カルボキシ末端を有するポリペプチドの調製 | |
EP0095351B1 (en) | A precursor of a c-terminal amidated peptide and production thereof | |
JPS6169788A (ja) | 修飾アデニン基を有するプローブ | |
US4728609A (en) | Recombinant growth hormone releasing factor | |
PT96224A (pt) | Producao de factor de crescimento derivado de plaquetas biologicamente activas a partir de sistema de celulas hospedeiras de elevada expressao | |
EP0107710A4 (en) | PRODUCTION AND EXPRESSION OF GENES FOR CALCITONIN AND ITS POLYPEPTIDE ANALOGS. | |
Nichifor et al. | Synthesis of peptide derivatives of 5-fluorouracil | |
US5474913A (en) | Process for the preparation of motilin-like polypeptide and expression thereof | |
JP2003508408A (ja) | 環状偽ペプチッドの製造方法 | |
JPS6069098A (ja) | セクレチンの調製法 | |
JP2575022B2 (ja) | ヒトモチリン前駆体、該前駆体含有クローン化dna、その調製法並びに該クローン化dnaが組込まれたプラスミド | |
US5459049A (en) | Motilin-like polypeptide and use thereof | |
US5252482A (en) | Precursor of a C-terminal amidated calcitonin | |
JP2561060B2 (ja) | 改良型rnアーゼt1 | |
CN111647049B (zh) | 多肽和多肽偶联物及其制备方法和应用 | |
JPS61286400A (ja) | 新規ペプチド |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MKLA | Lapsed | ||
MKLA | Lapsed |
Effective date: 19950812 |