FI104489B - Sian somatotropiineja, joissa on kaksoismutaatio alfakierteen 1 alueella - Google Patents
Sian somatotropiineja, joissa on kaksoismutaatio alfakierteen 1 alueella Download PDFInfo
- Publication number
- FI104489B FI104489B FI915654A FI915654A FI104489B FI 104489 B FI104489 B FI 104489B FI 915654 A FI915654 A FI 915654A FI 915654 A FI915654 A FI 915654A FI 104489 B FI104489 B FI 104489B
- Authority
- FI
- Finland
- Prior art keywords
- mutation
- somatotropin
- rpst
- dna
- helix
- Prior art date
Links
- 230000035772 mutation Effects 0.000 title claims abstract description 178
- 108010051696 Growth Hormone Proteins 0.000 claims abstract description 49
- 102000018997 Growth Hormone Human genes 0.000 claims abstract description 49
- 150000001413 amino acids Chemical class 0.000 claims abstract description 27
- 239000000203 mixture Substances 0.000 claims abstract description 19
- 230000004071 biological effect Effects 0.000 claims abstract description 8
- 239000012730 sustained-release form Substances 0.000 claims abstract description 7
- 238000009472 formulation Methods 0.000 claims abstract description 6
- 238000013268 sustained release Methods 0.000 claims abstract description 6
- 229940024606 amino acid Drugs 0.000 claims description 26
- 235000001014 amino acid Nutrition 0.000 claims description 26
- 235000018417 cysteine Nutrition 0.000 claims description 19
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 18
- 235000013922 glutamic acid Nutrition 0.000 claims description 18
- 239000004220 glutamic acid Substances 0.000 claims description 18
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 17
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 13
- 235000004279 alanine Nutrition 0.000 claims description 13
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 12
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 9
- 239000004475 Arginine Substances 0.000 claims description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 8
- 239000004472 Lysine Substances 0.000 claims description 8
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 8
- 235000009697 arginine Nutrition 0.000 claims description 8
- 235000018977 lysine Nutrition 0.000 claims description 8
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 7
- 235000004554 glutamine Nutrition 0.000 claims description 7
- 229960000310 isoleucine Drugs 0.000 claims description 7
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 7
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 6
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 5
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 5
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 4
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 4
- 239000004471 Glycine Substances 0.000 claims description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 3
- 241000282898 Sus scrofa Species 0.000 claims description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 3
- 239000004473 Threonine Substances 0.000 claims description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 3
- 235000003704 aspartic acid Nutrition 0.000 claims description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 3
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 3
- 235000014304 histidine Nutrition 0.000 claims description 3
- 229930182817 methionine Natural products 0.000 claims description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 2
- 235000009582 asparagine Nutrition 0.000 claims description 2
- 229960001230 asparagine Drugs 0.000 claims description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 2
- 239000004474 valine Substances 0.000 claims description 2
- 150000001945 cysteines Chemical class 0.000 claims 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 59
- 102000004169 proteins and genes Human genes 0.000 abstract description 21
- 238000000034 method Methods 0.000 abstract description 16
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 11
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 5
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 5
- 238000002741 site-directed mutagenesis Methods 0.000 abstract description 5
- 229920001184 polypeptide Polymers 0.000 abstract description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 102
- 239000013612 plasmid Substances 0.000 description 89
- 108020004414 DNA Proteins 0.000 description 87
- 239000012634 fragment Substances 0.000 description 45
- 108091028043 Nucleic acid sequence Proteins 0.000 description 43
- 231100000219 mutagenic Toxicity 0.000 description 35
- 230000003505 mutagenic effect Effects 0.000 description 35
- 231100000350 mutagenesis Toxicity 0.000 description 34
- 238000002703 mutagenesis Methods 0.000 description 33
- 238000006243 chemical reaction Methods 0.000 description 32
- 238000010276 construction Methods 0.000 description 32
- 238000009396 hybridization Methods 0.000 description 29
- 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 22
- 108020004705 Codon Proteins 0.000 description 21
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 20
- 239000000872 buffer Substances 0.000 description 20
- 235000018102 proteins Nutrition 0.000 description 20
- 108091008146 restriction endonucleases Proteins 0.000 description 20
- 239000000020 Nitrocellulose Substances 0.000 description 17
- 229920001220 nitrocellulos Polymers 0.000 description 17
- 239000000523 sample Substances 0.000 description 16
- 229960002989 glutamic acid Drugs 0.000 description 15
- 241001465754 Metazoa Species 0.000 description 14
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 14
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 14
- 230000001580 bacterial effect Effects 0.000 description 12
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 11
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 11
- 230000002209 hydrophobic effect Effects 0.000 description 11
- 238000011534 incubation Methods 0.000 description 11
- 239000013613 expression plasmid Substances 0.000 description 10
- 229910052757 nitrogen Inorganic materials 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 238000000246 agarose gel electrophoresis Methods 0.000 description 9
- 238000003556 assay Methods 0.000 description 9
- 239000011541 reaction mixture Substances 0.000 description 9
- 238000012216 screening Methods 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 8
- 239000000122 growth hormone Substances 0.000 description 8
- 102200082905 rs35203747 Human genes 0.000 description 8
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 102220220042 rs1060501784 Human genes 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 238000012300 Sequence Analysis Methods 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- 102000012410 DNA Ligases Human genes 0.000 description 5
- 108010061982 DNA Ligases Proteins 0.000 description 5
- 241000700159 Rattus Species 0.000 description 5
- 230000001976 improved effect Effects 0.000 description 5
- 108010083127 phage repressor proteins Proteins 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- ZKHQWZAMYRWXGA-KQYNXXCUSA-N Adenosine triphosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-N 0.000 description 4
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 4
- 108010017826 DNA Polymerase I Proteins 0.000 description 4
- 102000004594 DNA Polymerase I Human genes 0.000 description 4
- 102100028501 Galanin peptides Human genes 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 239000000543 intermediate Substances 0.000 description 4
- 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 4
- 230000001817 pituitary effect Effects 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 108010006025 bovine growth hormone Proteins 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 210000003608 fece Anatomy 0.000 description 3
- 230000005660 hydrophilic surface Effects 0.000 description 3
- 230000005661 hydrophobic surface Effects 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 3
- 238000003752 polymerase chain reaction Methods 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 102220074265 rs180177184 Human genes 0.000 description 3
- 102200090386 rs864309504 Human genes 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 2
- 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 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 101150094690 GAL1 gene Proteins 0.000 description 2
- 101150038242 GAL10 gene Proteins 0.000 description 2
- 102100024637 Galectin-10 Human genes 0.000 description 2
- 101100121078 Homo sapiens GAL gene Proteins 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 102000002265 Human Growth Hormone Human genes 0.000 description 2
- 239000000854 Human Growth Hormone Substances 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- 102000008300 Mutant Proteins Human genes 0.000 description 2
- 108010021466 Mutant Proteins Proteins 0.000 description 2
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 2
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 2
- 241000282887 Suidae Species 0.000 description 2
- 101150050575 URA3 gene Proteins 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 229960001456 adenosine triphosphate Drugs 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 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 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000004106 carminic acid Substances 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000003111 growth hormone derivative Substances 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000010871 livestock manure Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- 238000002515 oligonucleotide synthesis Methods 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 239000013615 primer Substances 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 101150116497 sacm1l gene Proteins 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 101150080291 ste7 gene Proteins 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- SVPKNMBRVBMTLB-UHFFFAOYSA-N 2,3-dichloronaphthalene-1,4-dione Chemical compound C1=CC=C2C(=O)C(Cl)=C(Cl)C(=O)C2=C1 SVPKNMBRVBMTLB-UHFFFAOYSA-N 0.000 description 1
- VPSXHKGJZJCWLV-UHFFFAOYSA-N 2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-3-(1-ethylpiperidin-4-yl)oxypyrazol-1-yl]-1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C=1C(=NN(C=1)CC(=O)N1CC2=C(CC1)NN=N2)OC1CCN(CC1)CC VPSXHKGJZJCWLV-UHFFFAOYSA-N 0.000 description 1
- CJRJTCMSQLEPFQ-UHFFFAOYSA-N 6-cat Chemical compound ClC1=CC=C2CC(N)CCC2=C1 CJRJTCMSQLEPFQ-UHFFFAOYSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- CXISPYVYMQWFLE-VKHMYHEASA-N Ala-Gly Chemical compound C[C@H]([NH3+])C(=O)NCC([O-])=O CXISPYVYMQWFLE-VKHMYHEASA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101100283604 Caenorhabditis elegans pigk-1 gene Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- XZMCDFZZKTWFGF-UHFFFAOYSA-N Cyanamide Chemical compound NC#N XZMCDFZZKTWFGF-UHFFFAOYSA-N 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 241001149900 Fusconaia subrotunda Species 0.000 description 1
- 102100040004 Gamma-glutamylcyclotransferase Human genes 0.000 description 1
- DSPQRJXOIXHOHK-WDSKDSINSA-N Glu-Asp-Gly Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O DSPQRJXOIXHOHK-WDSKDSINSA-N 0.000 description 1
- KOSRFJWDECSPRO-WDSKDSINSA-N Glu-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(O)=O KOSRFJWDECSPRO-WDSKDSINSA-N 0.000 description 1
- UQHGAYSULGRWRG-WHFBIAKZSA-N Glu-Ser Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CO)C(O)=O UQHGAYSULGRWRG-WHFBIAKZSA-N 0.000 description 1
- VHPVBPCCWVDGJL-IRIUXVKKSA-N Glu-Thr-Tyr Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O VHPVBPCCWVDGJL-IRIUXVKKSA-N 0.000 description 1
- OLIFSFOFKGKIRH-WUJLRWPWSA-N Gly-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)CN OLIFSFOFKGKIRH-WUJLRWPWSA-N 0.000 description 1
- 102100020948 Growth hormone receptor Human genes 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 101100246753 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) pyrF gene Proteins 0.000 description 1
- 101000886680 Homo sapiens Gamma-glutamylcyclotransferase Proteins 0.000 description 1
- 206010062767 Hypophysitis Diseases 0.000 description 1
- CTVJSFRHUOSCQQ-DCAQKATOSA-N Met-Arg-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O CTVJSFRHUOSCQQ-DCAQKATOSA-N 0.000 description 1
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- OKIZCWYLBDKLSU-UHFFFAOYSA-M N,N,N-Trimethylmethanaminium chloride Chemical compound [Cl-].C[N+](C)(C)C OKIZCWYLBDKLSU-UHFFFAOYSA-M 0.000 description 1
- 101100494726 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) pep-4 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
- 101100034381 Photobacterium phosphoreum ribE gene Proteins 0.000 description 1
- HMNSRTLZAJHSIK-YUMQZZPRSA-N Pro-Arg Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 HMNSRTLZAJHSIK-YUMQZZPRSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 108010068542 Somatotropin Receptors Proteins 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- BZTSQFWJNJYZSX-JRQIVUDYSA-N Thr-Tyr-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O BZTSQFWJNJYZSX-JRQIVUDYSA-N 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- PDSLRCZINIDLMU-QWRGUYRKSA-N Tyr-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 PDSLRCZINIDLMU-QWRGUYRKSA-N 0.000 description 1
- HPYDSVWYXXKHRD-VIFPVBQESA-N Tyr-Gly Chemical compound [O-]C(=O)CNC(=O)[C@@H]([NH3+])CC1=CC=C(O)C=C1 HPYDSVWYXXKHRD-VIFPVBQESA-N 0.000 description 1
- 108010047495 alanylglycine Proteins 0.000 description 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229940125898 compound 5 Drugs 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical group OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000000378 dietary effect Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001506 fluorescence spectroscopy Methods 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229940049906 glutamate Drugs 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-L glutamate group Chemical group N[C@@H](CCC(=O)[O-])C(=O)[O-] WHUUTDBJXJRKMK-VKHMYHEASA-L 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 230000002440 hepatic effect Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 125000000896 monocarboxylic acid group Chemical group 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 230000017066 negative regulation of growth Effects 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- JTJMJGYZQZDUJJ-UHFFFAOYSA-N phencyclidine Chemical compound C1CCCCN1C1(C=2C=CC=CC=2)CCCCC1 JTJMJGYZQZDUJJ-UHFFFAOYSA-N 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 210000003635 pituitary gland Anatomy 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 239000002798 polar solvent Substances 0.000 description 1
- 238000011176 pooling Methods 0.000 description 1
- 108010004914 prolylarginine Proteins 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 102220014802 rs45527543 Human genes 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 239000011734 sodium 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
- 229960004532 somatropin Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/27—Growth hormone [GH], i.e. somatotropin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Endocrinology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- General Chemical & Material Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Veterinary Medicine (AREA)
- Analytical Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Toxicology (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Secondary Cells (AREA)
- Mold Materials And Core Materials (AREA)
- Battery Electrode And Active Subsutance (AREA)
- Medicines Containing Plant Substances (AREA)
- Compositions Of Oxide Ceramics (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US62165690A | 1990-11-30 | 1990-11-30 | |
US62165690 | 1990-11-30 |
Publications (3)
Publication Number | Publication Date |
---|---|
FI915654A0 FI915654A0 (fi) | 1991-11-29 |
FI915654A FI915654A (fi) | 1992-05-31 |
FI104489B true FI104489B (fi) | 2000-02-15 |
Family
ID=24491070
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FI915654A FI104489B (fi) | 1990-11-30 | 1991-11-29 | Sian somatotropiineja, joissa on kaksoismutaatio alfakierteen 1 alueella |
Country Status (20)
Country | Link |
---|---|
US (1) | US5548068A (xx) |
EP (1) | EP0496973B1 (xx) |
JP (1) | JPH05105634A (xx) |
KR (1) | KR100193005B1 (xx) |
AT (1) | ATE163045T1 (xx) |
CA (1) | CA2056467C (xx) |
DE (1) | DE69128877T2 (xx) |
DK (1) | DK0496973T3 (xx) |
ES (1) | ES2112847T3 (xx) |
FI (1) | FI104489B (xx) |
GR (1) | GR3026761T3 (xx) |
HU (1) | HU215947B (xx) |
IE (1) | IE914153A1 (xx) |
IL (1) | IL100169A0 (xx) |
NO (1) | NO301235B1 (xx) |
NZ (2) | NZ260103A (xx) |
PT (1) | PT99648B (xx) |
SG (1) | SG49702A1 (xx) |
TW (1) | TW198040B (xx) |
ZA (1) | ZA919453B (xx) |
Families Citing this family (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6006079A (en) * | 1997-06-13 | 1999-12-21 | Motorola, Inc. | Radio having a fast adapting direct conversion receiver |
TR200504220T2 (tr) * | 1998-12-17 | 2007-04-24 | Biogen Idec Ma Inc. | Aktif limfotoksin-beta reseptör imunoglobülin şimeAktif limfotoksin-beta reseptör imunoglobülin şimerik proteinlerinin yüksek düzey ifadesi ve saflaştrik proteinlerinin yüksek düzey ifadesi ve saflaştırılması için bir yöntem.ırılması için bir yöntem. |
GB2389115B (en) * | 2001-12-14 | 2005-03-16 | Asterion Ltd | Polypeptide having a plurality of modified growth hormone receptor binding domains of growth hormone |
CA2498319A1 (en) * | 2002-09-09 | 2004-03-18 | Nautilus Biotech | Rational evolution of cytokines for higher stability, the cytokines and encoding nucleic acid molecules |
US7998930B2 (en) | 2004-11-04 | 2011-08-16 | Hanall Biopharma Co., Ltd. | Modified growth hormones |
US8338376B2 (en) | 2006-10-20 | 2012-12-25 | Biogen Idec Ma Inc. | Compositions comprising variant LT-B-R-IG fusion proteins |
MX2009004134A (es) | 2006-10-20 | 2009-08-12 | Biogen Idec Inc | Tratamiento de trastornos de desmielinizacion con el receptor de linfotoxina beta soluble. |
MX347038B (es) | 2011-02-23 | 2017-04-10 | Massachusetts Inst Technology | Proteínas de membrana solubles en agua y métodos para la preparación y uso de las mismas. |
US10373702B2 (en) | 2014-03-27 | 2019-08-06 | Massachusetts Institute Of Technology | Water-soluble trans-membrane proteins and methods for the preparation and use thereof |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0355460B1 (en) * | 1988-08-24 | 2000-12-27 | American Cyanamid Company | Stabilization of somatotropins by modification of cysteine residues utilizing site directed mutagenesis or chemical derivatization |
DE68929151T2 (de) * | 1988-10-28 | 2000-07-20 | Genentech, Inc. | Verfahren zum nachweis von aktiven domänen und aminosäureresten in polypeptiden und hormonvarianten |
-
1991
- 1991-11-25 NZ NZ260103A patent/NZ260103A/en unknown
- 1991-11-25 NZ NZ240718A patent/NZ240718A/en unknown
- 1991-11-27 IL IL100169A patent/IL100169A0/xx unknown
- 1991-11-28 DK DK91120396.6T patent/DK0496973T3/da active
- 1991-11-28 ES ES91120396T patent/ES2112847T3/es not_active Expired - Lifetime
- 1991-11-28 AT AT91120396T patent/ATE163045T1/de not_active IP Right Cessation
- 1991-11-28 EP EP91120396A patent/EP0496973B1/en not_active Expired - Lifetime
- 1991-11-28 DE DE69128877T patent/DE69128877T2/de not_active Expired - Fee Related
- 1991-11-28 SG SG1996004237A patent/SG49702A1/en unknown
- 1991-11-28 CA CA002056467A patent/CA2056467C/en not_active Expired - Fee Related
- 1991-11-29 FI FI915654A patent/FI104489B/fi active
- 1991-11-29 HU HU913723A patent/HU215947B/hu not_active IP Right Cessation
- 1991-11-29 JP JP3339516A patent/JPH05105634A/ja active Pending
- 1991-11-29 ZA ZA919453A patent/ZA919453B/xx unknown
- 1991-11-29 PT PT99648A patent/PT99648B/pt not_active IP Right Cessation
- 1991-11-29 IE IE415391A patent/IE914153A1/en not_active Application Discontinuation
- 1991-11-29 NO NO914724A patent/NO301235B1/no not_active IP Right Cessation
- 1991-11-30 KR KR1019910021901A patent/KR100193005B1/ko not_active IP Right Cessation
-
1992
- 1992-02-20 TW TW081101242A patent/TW198040B/zh active
-
1994
- 1994-12-23 US US08/363,982 patent/US5548068A/en not_active Expired - Fee Related
-
1998
- 1998-04-30 GR GR980400960T patent/GR3026761T3/el unknown
Also Published As
Publication number | Publication date |
---|---|
DE69128877D1 (de) | 1998-03-12 |
AU662493B2 (en) | 1995-09-07 |
ZA919453B (en) | 1992-08-26 |
AU8830091A (en) | 1992-06-04 |
DK0496973T3 (da) | 1998-05-04 |
JPH05105634A (ja) | 1993-04-27 |
HU913723D0 (en) | 1992-02-28 |
FI915654A (fi) | 1992-05-31 |
PT99648A (pt) | 1992-10-30 |
NZ240718A (en) | 1996-10-28 |
CA2056467A1 (en) | 1992-05-31 |
DE69128877T2 (de) | 1998-06-18 |
KR100193005B1 (ko) | 1999-06-15 |
HUT62327A (en) | 1993-04-28 |
SG49702A1 (en) | 1998-06-15 |
FI915654A0 (fi) | 1991-11-29 |
ES2112847T3 (es) | 1998-04-16 |
EP0496973A2 (en) | 1992-08-05 |
CA2056467C (en) | 1998-07-07 |
EP0496973A3 (en) | 1993-02-24 |
IL100169A0 (en) | 1992-08-18 |
NO914724L (no) | 1992-06-01 |
EP0496973B1 (en) | 1998-02-04 |
TW198040B (xx) | 1993-01-11 |
NO301235B1 (no) | 1997-09-29 |
NZ260103A (en) | 1996-10-28 |
GR3026761T3 (en) | 1998-07-31 |
ATE163045T1 (de) | 1998-02-15 |
HU215947B (hu) | 1999-03-29 |
KR920009413A (ko) | 1992-06-25 |
PT99648B (pt) | 1999-05-31 |
IE914153A1 (en) | 1992-06-03 |
US5548068A (en) | 1996-08-20 |
NO914724D0 (no) | 1991-11-29 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
DE69225432T2 (de) | A-C-B-Proinsulin, Verfahren zu seiner Herstellung und Verwendung, und Zwischenprodukte in der Insulin-Produktion | |
DE69434520T3 (de) | Biotinylierung von proteinen | |
PL158064B1 (pl) | Sposób wytwarzania ludzkiej proapolipoproteiny A-l PL PL PL PL PL PL PL PL | |
JPH02193A (ja) | ムテイン,dnaおよびその用途 | |
US5310882A (en) | Somatotropins with alterations in the α-helix 3 region | |
FI104489B (fi) | Sian somatotropiineja, joissa on kaksoismutaatio alfakierteen 1 alueella | |
EP0152333A2 (en) | Cardiac atrial peptides | |
DE69700561T2 (de) | Verfahren zur Entfernung von N-Terminalem Methionin | |
CA1340122C (en) | Modifications of somatotropins for enhanced stability | |
EP1066328B1 (en) | Chimeric protein containing an intramolecular chaperone-like sequence and its application to insulin production | |
JPH05271279A (ja) | ヒト副甲状腺ホルモンムテインおよびその製造法 | |
US4894362A (en) | Eel growth hormone | |
HU197939B (en) | Process for producing deoxyribonucleic acid, or its precursor, determining human growth hormone releasing factor | |
Mayne et al. | Direct expression of human growth in Escherichia coli with the lipoprotein promoter | |
NZ260176A (en) | Method for site directed mutagenesis on recombinantly derived polypeptide or protein and its application on somatotropin | |
US20020164712A1 (en) | Chimeric protein containing an intramolecular chaperone-like sequence | |
Phipps et al. | Retention of enzymatic activity by N-terminal domain (1–78) T4-lysozyme: Expression of synthetic DNA in Escherichiacoli | |
DE69006311T2 (de) | Antimetastatische peptide. | |
JPS62130697A (ja) | ペプチドの製造法 |