JP2013511997A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2013511997A5 JP2013511997A5 JP2012541487A JP2012541487A JP2013511997A5 JP 2013511997 A5 JP2013511997 A5 JP 2013511997A5 JP 2012541487 A JP2012541487 A JP 2012541487A JP 2012541487 A JP2012541487 A JP 2012541487A JP 2013511997 A5 JP2013511997 A5 JP 2013511997A5
- Authority
- JP
- Japan
- Prior art keywords
- xaa
- polypeptide
- peptide
- hydroxyglycine
- enzyme
- 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.)
- Granted
Links
- 108090000765 processed proteins & peptides Proteins 0.000 claims 32
- 102000004196 processed proteins & peptides Human genes 0.000 claims 21
- 229920001184 polypeptide Polymers 0.000 claims 19
- 102000004190 Enzymes Human genes 0.000 claims 12
- 108090000790 Enzymes Proteins 0.000 claims 12
- 150000001413 amino acids Chemical group 0.000 claims 10
- 241000894006 Bacteria Species 0.000 claims 8
- ZHWLPDIRXJCEJY-UHFFFAOYSA-N alpha-hydroxyglycine Chemical compound NC(O)C(O)=O ZHWLPDIRXJCEJY-UHFFFAOYSA-N 0.000 claims 7
- 238000006243 chemical reaction Methods 0.000 claims 6
- 230000000694 effects Effects 0.000 claims 6
- 102000004317 Lyases Human genes 0.000 claims 5
- 108090000856 Lyases Proteins 0.000 claims 5
- 238000000034 method Methods 0.000 claims 5
- 235000001014 amino acid Nutrition 0.000 claims 4
- 210000004027 cell Anatomy 0.000 claims 4
- 238000004519 manufacturing process Methods 0.000 claims 4
- 102100027467 Pro-opiomelanocortin Human genes 0.000 claims 3
- 210000004899 c-terminal region Anatomy 0.000 claims 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 3
- YNXLOPYTAAFMTN-SBUIBGKBSA-N C([C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)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](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)C1=CC=C(O)C=C1 Chemical compound C([C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)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](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)C1=CC=C(O)C=C1 YNXLOPYTAAFMTN-SBUIBGKBSA-N 0.000 claims 2
- 102000055006 Calcitonin Human genes 0.000 claims 2
- 108060001064 Calcitonin Proteins 0.000 claims 2
- 241000588724 Escherichia coli Species 0.000 claims 2
- 108010088406 Glucagon-Like Peptides Proteins 0.000 claims 2
- 101800001751 Melanocyte-stimulating hormone alpha Proteins 0.000 claims 2
- 108010088847 Peptide YY Proteins 0.000 claims 2
- 102100029909 Peptide YY Human genes 0.000 claims 2
- 108010069820 Pro-Opiomelanocortin Proteins 0.000 claims 2
- 239000000683 Pro-Opiomelanocortin Substances 0.000 claims 2
- 230000009435 amidation Effects 0.000 claims 2
- 238000007112 amidation reaction Methods 0.000 claims 2
- 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 claims 2
- 229960004015 calcitonin Drugs 0.000 claims 2
- 102000039446 nucleic acids Human genes 0.000 claims 2
- 108020004707 nucleic acids Proteins 0.000 claims 2
- 150000007523 nucleic acids Chemical class 0.000 claims 2
- 239000002773 nucleotide Substances 0.000 claims 2
- 125000003729 nucleotide group Chemical group 0.000 claims 2
- WHNFPRLDDSXQCL-UAZQEYIDSA-N α-msh Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(N)=O)NC(=O)[C@H](CO)NC(C)=O)C1=CC=C(O)C=C1 WHNFPRLDDSXQCL-UAZQEYIDSA-N 0.000 claims 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 1
- 102100038518 Calcitonin Human genes 0.000 claims 1
- 108090000932 Calcitonin Gene-Related Peptide Proteins 0.000 claims 1
- 102400000921 Gastrin Human genes 0.000 claims 1
- 108090001053 Gastrin releasing peptide Proteins 0.000 claims 1
- 102000004862 Gastrin releasing peptide Human genes 0.000 claims 1
- 108010052343 Gastrins Proteins 0.000 claims 1
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 claims 1
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 claims 1
- 241000124008 Mammalia Species 0.000 claims 1
- 101800000520 Melanotropin gamma Proteins 0.000 claims 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 claims 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 claims 1
- 101800000399 Neurokinin A Proteins 0.000 claims 1
- 102400000097 Neurokinin A Human genes 0.000 claims 1
- HEAUFJZALFKPBA-YRVBCFNBSA-N Neurokinin A Chemical compound C([C@@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)C(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC=1NC=NC=1)C(C)O)C1=CC=CC=C1 HEAUFJZALFKPBA-YRVBCFNBSA-N 0.000 claims 1
- 101800000989 Oxytocin Proteins 0.000 claims 1
- 102400000050 Oxytocin Human genes 0.000 claims 1
- XNOPRXBHLZRZKH-UHFFFAOYSA-N Oxytocin Natural products N1C(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CC(C)C)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C(C(C)CC)NC(=O)C1CC1=CC=C(O)C=C1 XNOPRXBHLZRZKH-UHFFFAOYSA-N 0.000 claims 1
- -1 PYY-3-36 Proteins 0.000 claims 1
- 102000018886 Pancreatic Polypeptide Human genes 0.000 claims 1
- 108700020479 Pancreatic hormone Proteins 0.000 claims 1
- 108010086019 Secretin Proteins 0.000 claims 1
- 102100037505 Secretin Human genes 0.000 claims 1
- GXBMIBRIOWHPDT-UHFFFAOYSA-N Vasopressin Natural products N1C(=O)C(CC=2C=C(O)C=CC=2)NC(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CCCN=C(N)N)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C1CC1=CC=CC=C1 GXBMIBRIOWHPDT-UHFFFAOYSA-N 0.000 claims 1
- 108010004977 Vasopressins Proteins 0.000 claims 1
- 102000002852 Vasopressins Human genes 0.000 claims 1
- KBZOIRJILGZLEJ-LGYYRGKSSA-N argipressin Chemical compound C([C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@@H](C(N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)=O)N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(N)=O)C1=CC=CC=C1 KBZOIRJILGZLEJ-LGYYRGKSSA-N 0.000 claims 1
- 230000003197 catalytic effect Effects 0.000 claims 1
- 238000005119 centrifugation Methods 0.000 claims 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 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 239000003814 drug Substances 0.000 claims 1
- PUBCCFNQJQKCNC-XKNFJVFFSA-N gastrin-releasingpeptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)C(C)C)[C@@H](C)O)C(C)C)[C@@H](C)O)C(C)C)C1=CNC=N1 PUBCCFNQJQKCNC-XKNFJVFFSA-N 0.000 claims 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims 1
- 239000001963 growth medium Substances 0.000 claims 1
- BPGXUIVWLQTVLZ-OFGSCBOVSA-N neuropeptide y(npy) Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 BPGXUIVWLQTVLZ-OFGSCBOVSA-N 0.000 claims 1
- XNOPRXBHLZRZKH-DSZYJQQASA-N oxytocin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@H](N)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)NCC(N)=O)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 XNOPRXBHLZRZKH-DSZYJQQASA-N 0.000 claims 1
- 229960001723 oxytocin Drugs 0.000 claims 1
- 125000001151 peptidyl group Chemical group 0.000 claims 1
- 229920001192 peptidylglycine Polymers 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 claims 1
- 229960002101 secretin Drugs 0.000 claims 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 claims 1
- 239000006228 supernatant Substances 0.000 claims 1
- 229960003726 vasopressin Drugs 0.000 claims 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP09177593.2 | 2009-12-01 | ||
| EP09177593 | 2009-12-01 | ||
| US26671109P | 2009-12-04 | 2009-12-04 | |
| US61/266,711 | 2009-12-04 | ||
| PCT/EP2010/068630 WO2011067283A1 (en) | 2009-12-01 | 2010-12-01 | Novel peptidyl alpha-hydroxyglycine alpha-amidating lyases |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2013511997A JP2013511997A (ja) | 2013-04-11 |
| JP2013511997A5 true JP2013511997A5 (enExample) | 2014-01-16 |
| JP5931738B2 JP5931738B2 (ja) | 2016-06-08 |
Family
ID=44114627
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2012541487A Expired - Fee Related JP5931738B2 (ja) | 2009-12-01 | 2010-12-01 | 新規のペプチジルアルファ−ヒドロキシグリシンアルファ−アミド化リアーゼ |
Country Status (6)
| Country | Link |
|---|---|
| US (2) | US9096843B2 (enExample) |
| EP (1) | EP2507258B1 (enExample) |
| JP (1) | JP5931738B2 (enExample) |
| CN (1) | CN102666570B (enExample) |
| ES (1) | ES2583259T3 (enExample) |
| WO (1) | WO2011067283A1 (enExample) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2015091131A1 (en) * | 2013-12-20 | 2015-06-25 | F. Hoffmann-La Roche Ag | Use of peptidylglycine alpha-amidating monooxigenase (pam) for c-terminal amidation |
| CN105985995A (zh) * | 2015-01-29 | 2016-10-05 | 暨南大学 | 一种利用家蚕生物反应器生产普兰林肽(pa)的方法 |
| CN113302310B (zh) * | 2018-12-18 | 2024-05-03 | 帕西昂奥地利有限两合公司 | 单步生物催化酰胺化 |
| CN110034855B (zh) * | 2019-04-10 | 2021-12-14 | 国网辽宁省电力有限公司 | 一种信息传输校验方法及系统 |
| CN115243709A (zh) * | 2020-02-26 | 2022-10-25 | Pam治疗诊断有限公司 | 肽酰甘氨酸α-酰胺化单加氧酶(PAM)用于治疗目的的用途 |
| US20230097988A1 (en) * | 2020-02-26 | 2023-03-30 | Pam Theragnostics Gmbh | Methods for determining peptidylglycine alpha-amidating monooxygenase (pam) and its use for diagnostic purpose |
| AU2021262609A1 (en) | 2020-05-01 | 2022-12-22 | Kashiv Biosciences, Llc | An improved process of purification of protein |
| EP4487124A4 (en) * | 2022-03-23 | 2026-03-04 | Kashiv Biosciences Llc | An improved process for the separation and analysis of pancreatic enzymes |
| WO2025133225A1 (en) * | 2023-12-22 | 2025-06-26 | Pam Theragnostics Gmbh | Pharmaceutical combination of peptide-gly and peptidylglycine alpha-amidating monooxygenase (pam) |
Family Cites Families (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4203570A (en) | 1978-08-23 | 1980-05-20 | The Western States Machine Company | Power-operated loading gate for centrifugal machines incorporating an auxiliary drive device |
| US4546082A (en) | 1982-06-17 | 1985-10-08 | Regents Of The Univ. Of California | E. coli/Saccharomyces cerevisiae plasmid cloning vector containing the alpha-factor gene for secretion and processing of hybrid proteins |
| US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
| WO1984004330A1 (en) | 1983-04-22 | 1984-11-08 | Amgen | Secretion of exogenous polypeptides from yeast |
| NZ207926A (en) | 1983-04-25 | 1988-04-29 | Genentech Inc | Use of yeast #a#-factor to assist in expression of proteins heterologus to yeast |
| US4870008A (en) | 1983-08-12 | 1989-09-26 | Chiron Corporation | Secretory expression in eukaryotes |
| US4931373A (en) | 1984-05-25 | 1990-06-05 | Zymogenetics, Inc. | Stable DNA constructs for expression of α-1 antitrypsin |
| DK58285D0 (da) | 1984-05-30 | 1985-02-08 | Novo Industri As | Peptider samt fremstilling og anvendelse deraf |
| US4708934A (en) | 1984-09-27 | 1987-11-24 | Unigene Laboratories, Inc. | α-amidation enzyme |
| US4766073A (en) | 1985-02-25 | 1988-08-23 | Zymogenetics Inc. | Expression of biologically active PDGF analogs in eucaryotic cells |
| US4885249A (en) | 1984-12-05 | 1989-12-05 | Allelix, Inc. | Aspergillus niger transformation system |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| EP0625577A1 (en) | 1985-08-29 | 1994-11-23 | Genencor International, Inc. | Heterologous polypeptides expressed in filamentous fungi, processes for their preparation, and vectors for their preparation |
| US4882279A (en) | 1985-10-25 | 1989-11-21 | Phillips Petroleum Company | Site selective genomic modification of yeast of the genus pichia |
| WO1987002670A1 (en) | 1985-10-25 | 1987-05-07 | Mackay Vivian L | Method of using bar1 for secreting foreign proteins |
| US4935349A (en) | 1986-01-17 | 1990-06-19 | Zymogenetics, Inc. | Expression of higher eucaryotic genes in aspergillus |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| GB8720115D0 (en) | 1987-08-26 | 1987-09-30 | Cooper G J S | Treatment of diabetes mellitus |
| US5789234A (en) | 1987-08-14 | 1998-08-04 | Unigene Laboratories, Inc. | Expression systems for amidating enzyme |
| JP2703598B2 (ja) | 1987-09-04 | 1998-01-26 | ノボ―ノルディスク アクティーゼルスカブ | アスペルギルス菌中でのタンパク質生産物の生産方法およびアスペルギルス菌中で使用するためのプロモーター |
| DK463887D0 (da) | 1987-09-07 | 1987-09-07 | Novo Industri As | Gaerleader |
| US6255067B1 (en) | 1987-09-15 | 2001-07-03 | The Johns Hopkins University | cDNA encoding peptidyl-glycine alpha-amidating monooxygenase (PAM) |
| US5037743A (en) | 1988-08-05 | 1991-08-06 | Zymogenetics, Inc. | BAR1 secretion signal |
| JP2845468B2 (ja) * | 1989-01-17 | 1999-01-13 | サントリー株式会社 | ヒト甲状腺由来Ｃ―末端α―アミド化酵素 |
| JP2535398B2 (ja) | 1989-01-17 | 1996-09-18 | サントリー株式会社 | アミド化ペプチドの製造方法 |
| EP0448513A3 (en) | 1990-03-21 | 1991-12-27 | Japat Ltd | Process for production of peptidylglycine alpha-hydroxylating monooxygenase and use thereof |
| ATE130368T1 (de) * | 1990-06-01 | 1995-12-15 | Japat Ltd | Peptdidylhydroxylglycine n-c lyase und dns dafür kodierend. |
| DK300090D0 (da) | 1990-12-19 | 1990-12-19 | Novo Nordisk As | Fremgangsmaade til fremstilling af leadersekvenser |
| US6495514B1 (en) * | 1998-01-21 | 2002-12-17 | Mercer University | Method for reducing inflammation and inducing an analgesic effect and compounds thereof |
| AU3274101A (en) * | 2000-01-06 | 2001-07-16 | Genoptera, Llc | Nucleic acids and polypeptides of invertebrate enzymes and methods of use |
| US7199217B2 (en) * | 2000-12-13 | 2007-04-03 | Eli Lilly And Company | Amidated glucagon-like peptide-1 |
| JP4716987B2 (ja) | 2003-07-23 | 2011-07-06 | ノバルティス アーゲー | 骨関節症におけるカルシトニンの使用 |
| JP5362349B2 (ja) | 2005-04-15 | 2013-12-11 | ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト | タンパク質を精製する方法 |
| EP1907561B1 (en) * | 2005-06-24 | 2013-08-28 | Unigene Laboratories, Inc. | Cell lines for expressing enzyme useful in the preparation of amidated products |
| ES2531372T3 (es) | 2006-10-13 | 2015-03-13 | Novo Nordisk Healthcare Ag | Enzimas de procesamiento fusionadas a marcadores de proteínas básicas |
| JP5401312B2 (ja) | 2007-06-29 | 2014-01-29 | 第一三共株式会社 | 組換えＣ−末端α−アミド化酵素誘導体 |
-
2010
- 2010-12-01 US US13/513,049 patent/US9096843B2/en not_active Expired - Fee Related
- 2010-12-01 WO PCT/EP2010/068630 patent/WO2011067283A1/en not_active Ceased
- 2010-12-01 EP EP10788057.7A patent/EP2507258B1/en not_active Not-in-force
- 2010-12-01 ES ES10788057.7T patent/ES2583259T3/es active Active
- 2010-12-01 JP JP2012541487A patent/JP5931738B2/ja not_active Expired - Fee Related
- 2010-12-01 CN CN201080054717.4A patent/CN102666570B/zh not_active Expired - Fee Related
-
2015
- 2015-06-30 US US14/755,183 patent/US20160083713A1/en not_active Abandoned
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2015531407A5 (enExample) | ||
| AU2009200783B2 (en) | Peptide amidation process | |
| CN107881187A (zh) | 将大肠杆菌表达的融合蛋白转化为利拉鲁肽的制备方法及应用 | |
| MY159074A (en) | Polypeptide having d-lactate dehydrogenase activity, polynucleotide encoding the polypeptide, and process for production of d-lactic acid | |
| US20160083713A1 (en) | Novel peptidyl alpha-hydroxyglycine alpha-amidating lyases | |
| CN113614113B (zh) | 含有荧光蛋白片段的融合蛋白及其用途 | |
| US12509665B2 (en) | Thioredoxin mutant, preparation method thereof, and application thereof in production of recombinant fusion protein | |
| AU2023204533A1 (en) | Linear polyfunctional multimer biomolecule coupled to polyubiquitin linker and use thereof | |
| JP2020513834A (ja) | ペプチドの発現および大規模生産 | |
| CN101490082A (zh) | 产生具有二碱基b链末端的胰岛素类似物的方法 | |
| MX2009004985A (es) | Secuencias para activar la expresión y control de las modificaciones de post-traducción de un polipéptido recombinante. | |
| EP2128252A1 (en) | Fused protein containing insulin precursor of overexpression and secretion type, dna encoding the same and method of producing insulin | |
| CN114651063B (zh) | 用于表达重组治疗性肽的n-末端延伸序列 | |
| TWI591177B (zh) | 一種胰高血糖素胜肽－２（ｇｌｐ－２）類似物的製備方法 | |
| KR20230165291A (ko) | 폴리펩티드의 발현 증가를 위한 구축물 및 방법 | |
| Yi et al. | Expression and purification of exendin-4 dimer in Escherichia coli and its interaction with GLP-1 receptor in vitro | |
| KR102857046B1 (ko) | 대장균을 이용한 글루카곤 호르몬 생산 시스템 | |
| JP2024537248A5 (enExample) | ||
| US20230272004A1 (en) | Ramp tag for insulin overexpression and method for manufacturing insulin using same | |
| WO2007005733A3 (en) | Novel peptides promoting neurite outgrowth | |
| KR20150123456A (ko) | 대장균 내 생산이 가능한 티모신 베타4 | |
| KR20150123455A (ko) | 효모를 이용한 티모신 베타4의 생산방법 | |
| HK1111426A1 (en) | Method for producing carboxy-terminal amidified peptides | |
| CA2789359A1 (en) | Chimeric surface active proteins | |
| HK1111426B (en) | Method for producing carboxy-terminal amidified peptides |