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 |
|---|---|---|---|---|
| RU2016129516A (ru) * | 2013-12-20 | 2018-01-25 | Ф. Хоффманн-Ля Рош Аг | ПРИМЕНЕНИЕ ПЕПТИДИЛГЛИЦИН-α-АМИДИРУЮЩЕЙ МОНООКСИДАЗЫ (РАМ) ДЛЯ С-КОНЦЕВОГО АМИДИРОВАНИЯ |
| 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 |
| EP3899003A1 (en) * | 2018-12-18 | 2021-10-27 | Patheon Austria GmbH & Co KG | Single step biocatalytic amidation |
| 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 |
| 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 |
| BR112022015949A2 (pt) * | 2020-02-26 | 2022-10-04 | Pam Theragnostics Gmbh | Peptidilglicina alfa-amidante mono-oxigenase (pam), seu uso, formulação farmacêutica, método para determinar a atividade de pam em uma amostra de fluido corporal de um indivíduo, e kits para realizar o método para diagnóstico, prognóstico ou prevenção de risco de uma doença em um indivíduo, para a detecção do nível de pam, e para realizar o método para determinar a atividade de pam |
| CA3182368A1 (en) | 2020-05-01 | 2021-11-04 | Kashiv Biosciences, Llc | An improved process of purification of protein |
| CA3255003A1 (en) * | 2022-03-23 | 2023-09-28 | Kashiv Biosciences Llc | IMPROVED METHOD FOR 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 |
| JPS60501140A (ja) | 1983-04-22 | 1985-07-25 | アムジエン | 酵母による外因性ポリペプチドの分泌 |
| 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 |
| UA41863C2 (uk) | 1985-10-25 | 2001-10-15 | Займодженетікс Інк. | Спосіб одержання гетерологічного поліпептиду в еукаріотичних мікроорганізмах |
| 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 |
| EP0383779B2 (en) | 1987-09-04 | 2000-05-31 | Novo Nordisk A/S | PROCESS FOR THE PRODUCTION OF PROTEIN PRODUCTS IN $i(ASPERGILLUS) AND PROMOTERS FOR USE IN $i(ASPERGILLUS) |
| 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 |
| 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 |
| 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 |
| EP0448513A3 (en) | 1990-03-21 | 1991-12-27 | Japat Ltd | Process for production of peptidylglycine alpha-hydroxylating monooxygenase and use thereof |
| ES2079054T3 (es) | 1990-06-01 | 1996-01-01 | Ciba Geigy Ag | Peptidilhidroxiglicina n-c-liasa y adn codificante de la misma. |
| 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 |
| WO2001049856A2 (en) | 2000-01-06 | 2001-07-12 | Genoptera, Llc | Drosophila enzymes, encoding nucleic acids and methods of use |
| EP1351984A2 (en) | 2000-12-13 | 2003-10-15 | Eli Lilly And Company | Amidated glucagon-like peptide-1 |
| KR101070036B1 (ko) | 2003-07-23 | 2011-10-04 | 노르딕 바이오사이언스 에이/에스 | 골관절염에 대한 칼시토닌의 용도 |
| EP1874798A1 (en) | 2005-04-15 | 2008-01-09 | Novo Nordisk A/S | Basic protein purification tags from thermophilic bacteria |
| US8815583B2 (en) | 2005-06-24 | 2014-08-26 | Enteris Biopharma, Inc. | Cell lines for expressing enzyme useful in the preparation of amidated products |
| WO2008043847A1 (en) | 2006-10-13 | 2008-04-17 | Novo Nordisk Health Care Ag | Processing enzymes fused to basic protein tags |
| CA2691374A1 (en) | 2007-06-29 | 2009-01-08 | Asubio Pharma Co., Ltd. | Recombinant c-terminal .alpha.-amidating enzyme derivative |
-
2010
- 2010-12-01 CN CN201080054717.4A patent/CN102666570B/zh not_active Expired - Fee Related
- 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 US US13/513,049 patent/US9096843B2/en not_active Expired - Fee Related
- 2010-12-01 EP EP10788057.7A patent/EP2507258B1/en not_active Not-in-force
- 2010-12-01 WO PCT/EP2010/068630 patent/WO2011067283A1/en not_active Ceased
-
2015
- 2015-06-30 US US14/755,183 patent/US20160083713A1/en not_active Abandoned
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2013511997A5 (enExample) | ||
| JP2015531407A5 (enExample) | ||
| RU2017123283A (ru) | Партнеры по слиянию для получения пептидов | |
| WO2020182229A1 (zh) | 一种融合蛋白及其制备利拉鲁肽中间体多肽的方法 | |
| AU2009200783B2 (en) | Peptide amidation process | |
| MY159074A (en) | Polypeptide having d-lactate dehydrogenase activity, polynucleotide encoding the polypeptide, and process for production of d-lactic acid | |
| JP2020513834A (ja) | ペプチドの発現および大規模生産 | |
| CN113614113B (zh) | 含有荧光蛋白片段的融合蛋白及其用途 | |
| CN101490082A (zh) | 产生具有二碱基b链末端的胰岛素类似物的方法 | |
| US20220411764A1 (en) | Thioredoxin mutant, preparation method thereof, and application thereof in production of recombinant fusion protein | |
| MX2009004985A (es) | Secuencias para activar la expresión y control de las modificaciones de post-traducción de un polipéptido recombinante. | |
| CN110835366B (zh) | 促进蛋白质可溶性表达的标签多肽及其用途 | |
| 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 | |
| RU2024117969A (ru) | Расщепленный с n-конца и/или c-конца растворимый полипептид ph20 и его применение | |
| US20230272004A1 (en) | Ramp tag for insulin overexpression and method for manufacturing insulin using same | |
| CN116063562A (zh) | 一种长效人重组胰高血糖素样肽-1及其应用 | |
| WO2022094146A1 (en) | Methods of converting precursor proteins to mature proteins using kex2 proteases | |
| CN119391659A (zh) | 多肽连接酶突变体及多肽的制备方法 | |
| WO2007005733A3 (en) | Novel peptides promoting neurite outgrowth | |
| KR20150123456A (ko) | 대장균 내 생산이 가능한 티모신 베타4 |