BE1001877A4 - Composes nouveaux. - Google Patents

Composes nouveaux. Download PDF

Info

Publication number: BE1001877A4
Authority: BE; Belgium
Prior art keywords: sep; amino acid; dna; prak; natural amino
Prior art date: 1988-02-25

Application number

BE8900189A

Other languages

English (en)

French (fr)

Original Assignee

Sandoz Sa

Priority date (The priority date 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 date listed.)

1988-02-25

Filing date

1989-02-24

Publication date

1990-04-03

1989-02-24 Application filed by Sandoz Sa filed Critical Sandoz Sa

1990-04-03 Application granted granted Critical

1990-04-03 Publication of BE1001877A4 publication Critical patent/BE1001877A4/fr

Links

150000001875 compounds Chemical class 0.000 title description 2
239000002158 endotoxin Substances 0.000 claims abstract description 142
150000001413 amino acids Chemical class 0.000 claims abstract description 119
108090000623 proteins and genes Proteins 0.000 claims abstract description 78
102000004169 proteins and genes Human genes 0.000 claims abstract description 35
230000000749 insecticidal effect Effects 0.000 claims abstract description 21
108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 12
108020004414 DNA Proteins 0.000 claims description 104
125000003275 alpha amino acid group Chemical group 0.000 claims description 58
239000002773 nucleotide Substances 0.000 claims description 39
125000003729 nucleotide group Chemical group 0.000 claims description 39
241000588724 Escherichia coli Species 0.000 claims description 37
238000000034 method Methods 0.000 claims description 34
241000238631 Hexapoda Species 0.000 claims description 20
239000000203 mixture Substances 0.000 claims description 17
230000008859 change Effects 0.000 claims description 13
238000007792 addition Methods 0.000 claims description 12
239000013604 expression vector Substances 0.000 claims description 12
230000002588 toxic effect Effects 0.000 claims description 12
238000012217 deletion Methods 0.000 claims description 10
230000037430 deletion Effects 0.000 claims description 10
230000001580 bacterial effect Effects 0.000 claims description 8
238000009396 hybridization Methods 0.000 claims description 6
238000012986 modification Methods 0.000 claims description 5
230000004048 modification Effects 0.000 claims description 5
238000001890 transfection Methods 0.000 claims description 2
230000001131 transforming effect Effects 0.000 claims description 2
238000012258 culturing Methods 0.000 claims 1
230000035772 mutation Effects 0.000 abstract description 71
108020004705 Codon Proteins 0.000 abstract description 25
238000004519 manufacturing process Methods 0.000 abstract description 11
241000193388 Bacillus thuringiensis Species 0.000 abstract description 3
229940097012 bacillus thuringiensis Drugs 0.000 abstract description 3
238000010188 recombinant method Methods 0.000 abstract description 3
108700003918 Bacillus Thuringiensis insecticidal crystal Proteins 0.000 abstract 1
BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 3224
239000013612 plasmid Substances 0.000 description 117
241000234435 Lilium Species 0.000 description 59
239000012634 fragment Substances 0.000 description 59
210000004027 cell Anatomy 0.000 description 53
230000000694 effects Effects 0.000 description 25
108091034117 Oligonucleotide Proteins 0.000 description 22
231100000419 toxicity Toxicity 0.000 description 21
230000001988 toxicity Effects 0.000 description 21
238000002360 preparation method Methods 0.000 description 18
239000000499 gel Substances 0.000 description 16
108091008146 restriction endonucleases Proteins 0.000 description 15
239000013598 vector Substances 0.000 description 15
101100016593 Encephalitozoon cuniculi (strain GB-M1) HD-1 gene Proteins 0.000 description 13
238000003776 cleavage reaction Methods 0.000 description 13
238000002474 experimental method Methods 0.000 description 13
230000007017 scission Effects 0.000 description 13
230000001174 ascending effect Effects 0.000 description 11
241001607516 Thelohanellus wuhanensis Species 0.000 description 10
239000002253 acid Substances 0.000 description 10
239000002775 capsule Substances 0.000 description 10
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 9
241000193830 Bacillus <bacterium> Species 0.000 description 9
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
231100000331 toxic Toxicity 0.000 description 9
238000011144 upstream manufacturing Methods 0.000 description 9
102000053602 DNA Human genes 0.000 description 8
241000196324 Embryophyta Species 0.000 description 8
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 8
239000000074 antisense oligonucleotide Substances 0.000 description 8
238000012230 antisense oligonucleotides Methods 0.000 description 8
239000000843 powder Substances 0.000 description 8
239000003053 toxin Substances 0.000 description 8
231100000765 toxin Toxicity 0.000 description 8
108700012359 toxins Proteins 0.000 description 8
241000894006 Bacteria Species 0.000 description 7
229960005091 chloramphenicol Drugs 0.000 description 7
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 7
238000011156 evaluation Methods 0.000 description 7
229920001817 Agar Polymers 0.000 description 6
241000255777 Lepidoptera Species 0.000 description 6
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 6
239000008272 agar Substances 0.000 description 6
150000001412 amines Chemical class 0.000 description 6
125000000539 amino acid group Chemical group 0.000 description 6
230000000692 anti-sense effect Effects 0.000 description 6
239000000047 product Substances 0.000 description 6
238000011160 research Methods 0.000 description 6
239000000126 substance Substances 0.000 description 6
238000012360 testing method Methods 0.000 description 6
230000009466 transformation Effects 0.000 description 6
229960000723 ampicillin Drugs 0.000 description 5
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 5
239000012141 concentrate Substances 0.000 description 5
238000011534 incubation Methods 0.000 description 5
239000002917 insecticide Substances 0.000 description 5
210000000936 intestine Anatomy 0.000 description 5
238000002955 isolation Methods 0.000 description 5
210000003705 ribosome Anatomy 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
108091026890 Coding region Proteins 0.000 description 4
241001555556 Ephestia elutella Species 0.000 description 4
235000010469 Glycine max Nutrition 0.000 description 4
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
241000364057 Peoria Species 0.000 description 4
102000007562 Serum Albumin Human genes 0.000 description 4
108010071390 Serum Albumin Proteins 0.000 description 4
108020004682 Single-Stranded DNA Proteins 0.000 description 4
235000015278 beef Nutrition 0.000 description 4
238000006243 chemical reaction Methods 0.000 description 4
230000000295 complement effect Effects 0.000 description 4
230000029087 digestion Effects 0.000 description 4
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 4
238000001962 electrophoresis Methods 0.000 description 4
235000013305 food Nutrition 0.000 description 4
229910001629 magnesium chloride Inorganic materials 0.000 description 4
229930182817 methionine Natural products 0.000 description 4
231100000219 mutagenic Toxicity 0.000 description 4
230000003505 mutagenic effect Effects 0.000 description 4
230000001105 regulatory effect Effects 0.000 description 4
239000000523 sample Substances 0.000 description 4
238000012163 sequencing technique Methods 0.000 description 4
238000013207 serial dilution Methods 0.000 description 4
238000006467 substitution reaction Methods 0.000 description 4
238000012546 transfer Methods 0.000 description 4
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 4
102000012410 DNA Ligases Human genes 0.000 description 3
108010061982 DNA Ligases Proteins 0.000 description 3
238000001712 DNA sequencing Methods 0.000 description 3
108010042407 Endonucleases Proteins 0.000 description 3
102000004533 Endonucleases Human genes 0.000 description 3
102000004190 Enzymes Human genes 0.000 description 3
108090000790 Enzymes Proteins 0.000 description 3
102100026038 Lens fiber membrane intrinsic protein Human genes 0.000 description 3
101710115990 Lens fiber membrane intrinsic protein Proteins 0.000 description 3
108091000080 Phosphotransferase Proteins 0.000 description 3
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 3
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 3
241000255993 Trichoplusia ni Species 0.000 description 3
239000011543 agarose gel Substances 0.000 description 3
108020001507 fusion proteins Proteins 0.000 description 3
102000037865 fusion proteins Human genes 0.000 description 3
230000002068 genetic effect Effects 0.000 description 3
231100000171 higher toxicity Toxicity 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
239000012071 phase Substances 0.000 description 3
102000020233 phosphotransferase Human genes 0.000 description 3
238000000746 purification Methods 0.000 description 3
239000012475 sodium chloride buffer Substances 0.000 description 3
239000000243 solution Substances 0.000 description 3
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 2
FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 description 2
241000255925 Diptera Species 0.000 description 2
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
108091027305 Heteroduplex Proteins 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 2
239000000908 ammonium hydroxide Substances 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
239000000872 buffer Substances 0.000 description 2
230000010261 cell growth Effects 0.000 description 2
238000010367 cloning Methods 0.000 description 2
238000001816 cooling Methods 0.000 description 2
238000011161 development Methods 0.000 description 2
230000018109 developmental process Effects 0.000 description 2
238000010790 dilution Methods 0.000 description 2
239000012895 dilution Substances 0.000 description 2
231100000673 dose–response relationship Toxicity 0.000 description 2
230000008030 elimination Effects 0.000 description 2
238000003379 elimination reaction Methods 0.000 description 2
238000000855 fermentation Methods 0.000 description 2
230000004151 fermentation Effects 0.000 description 2
239000012467 final product Substances 0.000 description 2
OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 2
230000037406 food intake Effects 0.000 description 2
230000012010 growth Effects 0.000 description 2
238000010348 incorporation Methods 0.000 description 2
230000000977 initiatory effect Effects 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
239000000463 material Substances 0.000 description 2
231100000350 mutagenesis Toxicity 0.000 description 2
238000002703 mutagenesis Methods 0.000 description 2
235000015097 nutrients Nutrition 0.000 description 2
239000008188 pellet Substances 0.000 description 2
238000006116 polymerization reaction Methods 0.000 description 2
230000010076 replication Effects 0.000 description 2
230000003362 replicative effect Effects 0.000 description 2
238000012216 screening Methods 0.000 description 2
230000028070 sporulation Effects 0.000 description 2
238000001694 spray drying Methods 0.000 description 2
238000010561 standard procedure Methods 0.000 description 2
235000013343 vitamin Nutrition 0.000 description 2
239000011782 vitamin Substances 0.000 description 2
229940088594 vitamin Drugs 0.000 description 2
229930003231 vitamin Natural products 0.000 description 2
150000003722 vitamin derivatives Chemical class 0.000 description 2
YZZUQHDYJXWFNG-VVEMGJRMSA-N (1S,2R,3S,3'S,5R,6S,7R,8S,9R,12R)-2,8-dihydroxy-3'-[(1S)-1-hydroxyethyl]-7-methyl-12-prop-1-en-2-ylspiro[4,10-dioxatetracyclo[7.2.1.02,7.03,5]dodecane-6,5'-oxolane]-2',11-dione Chemical compound C[C@@H]([C@@H]1C[C@]2([C@H]3[C@H](O3)[C@@]4([C@]2([C@@H]([C@H]5[C@H]([C@@H]4C(=O)O5)C(=C)C)O)C)O)OC1=O)O YZZUQHDYJXWFNG-VVEMGJRMSA-N 0.000 description 1
GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 description 1
OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
241000589155 Agrobacterium tumefaciens Species 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
108020000948 Antisense Oligonucleotides Proteins 0.000 description 1
235000014469 Bacillus subtilis Nutrition 0.000 description 1
235000017647 Brassica oleracea var italica Nutrition 0.000 description 1
244000308180 Brassica oleracea var. italica Species 0.000 description 1
108091028026 C-DNA Proteins 0.000 description 1
101100268668 Caenorhabditis elegans acc-2 gene Proteins 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
241000282836 Camelus dromedarius Species 0.000 description 1
240000001817 Cereus hexagonus Species 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
241000254173 Coleoptera Species 0.000 description 1
244000124209 Crocus sativus Species 0.000 description 1
101710151559 Crystal protein Proteins 0.000 description 1
AUNGANRZJHBGPY-UHFFFAOYSA-N D-Lyxoflavin Natural products OCC(O)C(O)C(O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-UHFFFAOYSA-N 0.000 description 1
102000004594 DNA Polymerase I Human genes 0.000 description 1
108010017826 DNA Polymerase I Proteins 0.000 description 1
230000009946 DNA mutation Effects 0.000 description 1
230000006820 DNA synthesis Effects 0.000 description 1
101100058504 Drosophila melanogaster Muted gene Proteins 0.000 description 1
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 1
241001524679 Escherichia virus M13 Species 0.000 description 1
206010056740 Genital discharge Diseases 0.000 description 1
244000068988 Glycine max Species 0.000 description 1
206010053759 Growth retardation Diseases 0.000 description 1
101150107978 HD-1 gene Proteins 0.000 description 1
241000256244 Heliothis virescens Species 0.000 description 1
108010042653 IgA receptor Proteins 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 1
101100442582 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) spe-1 gene Proteins 0.000 description 1
101710163270 Nuclease Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
YZZUQHDYJXWFNG-UHFFFAOYSA-N Pretoxin Natural products CC(O)C1CC2(OC1=O)C1OC1C1(O)C3C(C(OC3=O)C(O)C21C)C(C)=C YZZUQHDYJXWFNG-UHFFFAOYSA-N 0.000 description 1
102100034014 Prolyl 3-hydroxylase 3 Human genes 0.000 description 1
239000004365 Protease Substances 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
108020004511 Recombinant DNA Proteins 0.000 description 1
108091081021 Sense strand Proteins 0.000 description 1
241000256103 Simuliidae Species 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
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 1
241000209140 Triticum Species 0.000 description 1
235000021307 Triticum Nutrition 0.000 description 1
108091023045 Untranslated Region Proteins 0.000 description 1
229930003779 Vitamin B12 Natural products 0.000 description 1
DFPAKSUCGFBDDF-ZQBYOMGUSA-N [14c]-nicotinamide Chemical compound N[14C](=O)C1=CC=CN=C1 DFPAKSUCGFBDDF-ZQBYOMGUSA-N 0.000 description 1
206010000059 abdominal discomfort Diseases 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
230000009471 action Effects 0.000 description 1
239000013543 active substance Substances 0.000 description 1
239000000654 additive Substances 0.000 description 1
230000000996 additive effect Effects 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
235000021405 artificial diet Nutrition 0.000 description 1
238000003556 assay Methods 0.000 description 1
210000003719 b-lymphocyte Anatomy 0.000 description 1
102000023732 binding proteins Human genes 0.000 description 1
108091008324 binding proteins Proteins 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
229960002685 biotin Drugs 0.000 description 1
235000020958 biotin Nutrition 0.000 description 1
239000011616 biotin Substances 0.000 description 1
101150086827 bloc1s5 gene Proteins 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
239000011575 calcium Substances 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 1
238000010276 construction Methods 0.000 description 1
238000005520 cutting process Methods 0.000 description 1
SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
230000018044 dehydration Effects 0.000 description 1
238000006297 dehydration reaction Methods 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000000502 dialysis Methods 0.000 description 1
235000005911 diet Nutrition 0.000 description 1
230000037213 diet Effects 0.000 description 1
239000012153 distilled water Substances 0.000 description 1
229940079593 drug Drugs 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000001035 drying Methods 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
230000002346 endotoxic effect Effects 0.000 description 1
BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 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
230000001747 exhibiting effect Effects 0.000 description 1
235000013312 flour Nutrition 0.000 description 1
229960000304 folic acid Drugs 0.000 description 1
235000019152 folic acid Nutrition 0.000 description 1
239000011724 folic acid Substances 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
239000003292 glue Substances 0.000 description 1
231100000001 growth retardation Toxicity 0.000 description 1
238000003306 harvesting Methods 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
238000005286 illumination Methods 0.000 description 1
238000003119 immunoblot Methods 0.000 description 1
239000004615 ingredient Substances 0.000 description 1
230000001418 larval effect Effects 0.000 description 1
238000009630 liquid culture Methods 0.000 description 1
238000012423 maintenance Methods 0.000 description 1
238000013507 mapping Methods 0.000 description 1
230000021121 meiosis Effects 0.000 description 1
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
244000005700 microbiome Species 0.000 description 1
238000000520 microinjection Methods 0.000 description 1
230000003278 mimic effect Effects 0.000 description 1
230000011278 mitosis Effects 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
230000000869 mutational effect Effects 0.000 description 1
RZSCFTDHFNHMOR-UHFFFAOYSA-N n-(2,4-difluorophenyl)-2-[3-(trifluoromethyl)phenoxy]pyridine-3-carboxamide;1,1-dimethyl-3-(4-propan-2-ylphenyl)urea Chemical compound CC(C)C1=CC=C(NC(=O)N(C)C)C=C1.FC1=CC(F)=CC=C1NC(=O)C1=CC=CN=C1OC1=CC=CC(C(F)(F)F)=C1 RZSCFTDHFNHMOR-UHFFFAOYSA-N 0.000 description 1
235000014571 nuts Nutrition 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
229920003023 plastic Polymers 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
239000002243 precursor Substances 0.000 description 1
230000008569 process Effects 0.000 description 1
231100000654 protein toxin Toxicity 0.000 description 1
230000006337 proteolytic cleavage Effects 0.000 description 1
ZUFQODAHGAHPFQ-UHFFFAOYSA-N pyridoxine hydrochloride Chemical compound Cl.CC1=NC=C(CO)C(CO)=C1O ZUFQODAHGAHPFQ-UHFFFAOYSA-N 0.000 description 1
229960004172 pyridoxine hydrochloride Drugs 0.000 description 1
235000019171 pyridoxine hydrochloride Nutrition 0.000 description 1
239000011764 pyridoxine hydrochloride Substances 0.000 description 1
230000008929 regeneration Effects 0.000 description 1
238000011069 regeneration method Methods 0.000 description 1
229960002477 riboflavin Drugs 0.000 description 1
235000019192 riboflavin Nutrition 0.000 description 1
239000002151 riboflavin Substances 0.000 description 1
239000011833 salt mixture Substances 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000012882 sequential analysis Methods 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
238000010532 solid phase synthesis reaction Methods 0.000 description 1
238000007711 solidification Methods 0.000 description 1
230000008023 solidification Effects 0.000 description 1
235000010199 sorbic acid Nutrition 0.000 description 1
239000004334 sorbic acid Substances 0.000 description 1
229940075582 sorbic acid Drugs 0.000 description 1
238000005507 spraying Methods 0.000 description 1
238000010186 staining Methods 0.000 description 1
238000003756 stirring Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
231100000820 toxicity test Toxicity 0.000 description 1
230000003612 virological effect Effects 0.000 description 1
230000000007 visual effect Effects 0.000 description 1
239000011715 vitamin B12 Substances 0.000 description 1
235000019163 vitamin B12 Nutrition 0.000 description 1
238000001262 western blot Methods 0.000 description 1
239000004563 wettable powder Substances 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/32—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Bacillus (G)
- C07K14/325—Bacillus thuringiensis crystal peptides, i.e. delta-endotoxins
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
- A01N63/50—Isolated enzymes; Isolated proteins

Landscapes

Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
General Health & Medical Sciences (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Zoology (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
Agronomy & Crop Science (AREA)
Virology (AREA)
Molecular Biology (AREA)
Genetics & Genomics (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Gastroenterology & Hepatology (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Pest Control & Pesticides (AREA)
Plant Pathology (AREA)
Medicinal Chemistry (AREA)
Crystallography & Structural Chemistry (AREA)
Dentistry (AREA)
Wood Science & Technology (AREA)
Environmental Sciences (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)

BE8900189A 1988-02-25 1989-02-24 Composes nouveaux. BE1001877A4 (fr)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US16023388A	1988-02-25	1988-02-25

Publications (1)

Publication Number	Publication Date
BE1001877A4 true BE1001877A4 (fr)	1990-04-03

Family

ID=22576065

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
BE8900189A BE1001877A4 (fr)	1988-02-25	1989-02-24	Composes nouveaux.

Country Status (23)

Country	Link
JP (1)	JPH025872A (de)
CN (1)	CN1037538A (de)
AT (1)	AT396940B (de)
AU (1)	AU616945B2 (de)
BE (1)	BE1001877A4 (de)
BR (1)	BR8900881A (de)
DE (1)	DE3905865A1 (de)
DK (1)	DK84589A (de)
ES (1)	ES2012283A6 (de)
FR (1)	FR2627778B1 (de)
GB (1)	GB2216127B (de)
GR (1)	GR1000457B (de)
HU (1)	HU209148B (de)
IE (1)	IE62118B1 (de)
IL (1)	IL89391A (de)
IT (1)	IT1230483B (de)
MY (1)	MY104405A (de)
NL (1)	NL8900481A (de)
NZ (1)	NZ228108A (de)
PL (1)	PL161726B1 (de)
PT (1)	PT89812B (de)
TR (1)	TR26073A (de)
ZA (1)	ZA891463B (de)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB8910624D0 (en) *	1989-05-09	1989-06-21	Ici Plc	Bacterial strains
EP0433945A3 (en) *	1989-12-18	1991-10-23	Sandoz Ltd.	Insecticides produced by transformation of b.t. kurstaki with heterologeous genes
GB9408466D0 (en) *	1994-04-27	1994-06-22	Univ Nottingham	Cloning and functional expression of neurotoxins
CA2234656C (en) *	1995-10-13	2008-01-08	Dow Agrosciences Llc	Modified bacillus thuringiensis gene for lepidopteran control in plants
DE10011300A1 (de)	1999-03-10	2000-09-14	Sumitomo Spec Metals	Mahlvorrichtung und Mahlverfahren zum Herstellen von Pulver
JP4855772B2 (ja) *	2005-12-21	2012-01-18	ノリタケ伊勢電子株式会社	蛍光表示装置
JP4753987B2 (ja)	2008-11-10	2011-08-24	双葉電子工業株式会社	蛍光表示管及び駆動方法

Citations (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0186379B1 (de) *	1984-12-12	1991-03-13	Suntory Limited	Gen für ein Protein mit insektizider Wirkung

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0206613B1 (de) *	1985-06-14	1992-08-19	Repligen Corporation	Aktiviertes Bacillus thuringiensis-Delta-Endotoxin, hergestellt von einem manipulierten Hybrid-Gen
CA1341092C (en) *	1985-12-12	2000-09-05	David L. Edwards	Process for altering the host range of bacillus thuringiensis toxins, and novel toxins produced thereby
SG43288A1 (en) *	1987-04-16	1997-10-17	Ecogen Inc	Bacillus thuringiensis p-2 toxin gene protein and related insecticide compositions

1989
- 1989-01-27 BR BR898900881A patent/BR8900881A/pt not_active IP Right Cessation
- 1989-02-15 HU HU89760A patent/HU209148B/hu not_active IP Right Cessation
- 1989-02-22 IT IT8947678A patent/IT1230483B/it active
- 1989-02-22 GB GB8904016A patent/GB2216127B/en not_active Expired - Lifetime
- 1989-02-23 PT PT89812A patent/PT89812B/pt not_active IP Right Cessation
- 1989-02-23 IL IL8939189A patent/IL89391A/en not_active IP Right Cessation
- 1989-02-23 DK DK084589A patent/DK84589A/da not_active Application Discontinuation
- 1989-02-23 JP JP1044989A patent/JPH025872A/ja active Pending
- 1989-02-23 AU AU30297/89A patent/AU616945B2/en not_active Ceased
- 1989-02-23 GR GR890100115A patent/GR1000457B/el unknown
- 1989-02-23 NZ NZ228108A patent/NZ228108A/en unknown
- 1989-02-24 AT AT0041389A patent/AT396940B/de not_active IP Right Cessation
- 1989-02-24 MY MYPI89000227A patent/MY104405A/en unknown
- 1989-02-24 ES ES8900683A patent/ES2012283A6/es not_active Expired - Lifetime
- 1989-02-24 TR TR89/0166A patent/TR26073A/xx unknown
- 1989-02-24 PL PL89277925A patent/PL161726B1/pl unknown
- 1989-02-24 FR FR8902428A patent/FR2627778B1/fr not_active Expired - Lifetime
- 1989-02-24 DE DE3905865A patent/DE3905865A1/de not_active Withdrawn
- 1989-02-24 IE IE58989A patent/IE62118B1/en not_active IP Right Cessation
- 1989-02-24 CN CN89101863A patent/CN1037538A/zh active Pending
- 1989-02-24 BE BE8900189A patent/BE1001877A4/fr not_active IP Right Cessation
- 1989-02-24 ZA ZA891463A patent/ZA891463B/xx unknown
- 1989-02-27 NL NL8900481A patent/NL8900481A/nl not_active Application Discontinuation

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0186379B1 (de) *	1984-12-12	1991-03-13	Suntory Limited	Gen für ein Protein mit insektizider Wirkung

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
GENE, vol. 48, 1986, pages 109-118, Elsevier Science Publishers B.V. (Biomedical Division), Amsterdam, NL; M. GEISER et al.: "The hypervariable region in the genes coding for entomopathogenic crystal proteins of Bacillus thuringiensis: nucleotide sequence of the kurhd1 gene of subsp. kurstaki HD1" *
MICROBIOLOGICAL REVIEWS, vol. 50, no. 1, mars 1986, pages 1-24, American Society for Microbiology; A.I. ARONSON et al.: "Bacillus thuringiensis and related insect pathogens" *
NATURE, vol. 328, 2 juillet 1987, pages 33-37; M. VAECK et al.: "Transgenic plants protected from insect attack" *

Also Published As

Publication number	Publication date
IT1230483B (it)	1991-10-24
DK84589D0 (da)	1989-02-23
IT8947678A0 (it)	1989-02-22
MY104405A (en)	1994-03-31
AU3029789A (en)	1989-10-12
GB8904016D0 (en)	1989-04-05
DE3905865A1 (de)	1989-09-07
PL161726B1 (pl)	1993-07-30
GB2216127B (en)	1991-11-06
AU616945B2 (en)	1991-11-14
HU209148B (en)	1994-03-28
IE890589L (en)	1989-08-25
PT89812B (pt)	1994-04-29
HUT50507A (en)	1990-02-28
ES2012283A6 (es)	1990-03-01
FR2627778A1 (fr)	1989-09-01
PT89812A (pt)	1989-10-04
FR2627778B1 (fr)	1990-09-21
PL277925A1 (en)	1990-02-05
IL89391A (en)	1995-01-24
JPH025872A (ja)	1990-01-10
IL89391A0 (en)	1989-09-10
GB2216127A (en)	1989-10-04
AT396940B (de)	1993-12-27
NL8900481A (nl)	1989-09-18
ZA891463B (en)	1990-10-31
DK84589A (da)	1989-08-26
IE62118B1 (en)	1994-12-14
TR26073A (tr)	1993-12-16
CN1037538A (zh)	1989-11-29
BR8900881A (pt)	1989-10-17
NZ228108A (en)	1992-04-28
ATA41389A (de)	1993-05-15
GR1000457B (el)	1992-07-30

Legal Events

Date

Code

Title

Description

1996-08-31

RE

Patent lapsed

Owner name: S.A. SANDOZ

Effective date: 19960228

Publication	Publication Date	Title
AU729228B2 (en)	2001-01-25	Insecticidal protein toxins from photorhabdus
CA2162158A1 (fr)	1994-11-10	Sequences de nucleotides pour le controle de l'expression de sequences d'adn dans un hote cellulaire
JPH10506532A (ja)	1998-06-30	新規な有害生物防除性タンパク質および菌株
JP4338057B2 (ja)	2009-09-30	殺虫剤
FR2534594A1 (fr)	1984-04-20	Muteines appauvries en cysteine provenant de proteines biologiquement actives, adn codant pour ces muteines, vecteurs d'expression et cellules contenant cet adn, leurs procedes d'obtention et compositions therapeutiques contenant ces muteines
BE1001877A4 (fr)	1990-04-03	Composes nouveaux.
FR2525630A1 (fr)	1983-10-28	Adn contenant une sequence codant pour une proteine du cristal ou un polypeptide doue de proprietes insecticides, micro-organismes transformes par de tels adn, compositions contenant lesdites proteines du cristal, polypeptide ou micro-organismes
CA2409940C (fr)	2012-05-15	Bacteriocine anti-listeria
BR112020026523A2 (pt)	2021-04-06	Proteínas inibidoras de inseto
EP0295156B1 (de)	1995-04-26	Nukleotidsequenzen, die für mit larvizider Aktivität gegenüber Lepidopteren ausgestattete Polypeptide kodieren
JP2531913B2 (ja)	1996-09-04	バシルスチュリンギエンシス（Ｂａｓｉｌｌｕｓｔｈｕｒｉｎｇｉｅｎｓｉｓ）ｃｒｙＩＩＩＣ（ｂ）毒素遺伝子及び甲虫類昆虫に毒性のタンパク質
Zhang et al.	2019	Mating-type loci of Ustilago esculenta are essential for mating and development
KR102286087B1 (ko)	2021-08-05	클라미도모나스 변이주 및 이의 용도
JPH08509608A (ja)	1996-10-15	殺虫性蛋白コード化遺伝子含有組込みｄｎａセグメント
EP0777734B1 (de)	2006-03-08	Neue polypeptide mit toxischer aktivität gegen insekten der familie der dipteren
EP0411115A1 (de)	1991-02-06	Expression von nukleotiden sequenzen, die für gasvesikel kodieren
WO1988009812A1 (fr)	1988-12-15	Sequences de nucleotidiques codant pour des polypeptides dotes d'une activite larvicide vis-a-vis de lepidopteres
CA2418365A1 (en)	2002-02-21	Methods for blocking resistance to bt toxins in insects and nematodes
Hartzell	2002	Genetic tools for dissecting motility and development of Myxococcus xanthus
EP0323489A1 (de)	1989-07-12	Herstellung neuer proteinsüssmittel
Teintze et al.	1991	A development-specific Ca2+-binding protein from Myxococcus xanthus
US20030213012A1 (en)	2003-11-13	Pesticidal agents
JPH08510637A (ja)	1996-11-12	バチルス・チュリンゲンシスの新菌株及びその殺虫性タンパク質