CH675879A5 - - Google Patents
Download PDFInfo
- Publication number
- CH675879A5 CH675879A5 CH3045/88A CH304588A CH675879A5 CH 675879 A5 CH675879 A5 CH 675879A5 CH 3045/88 A CH3045/88 A CH 3045/88A CH 304588 A CH304588 A CH 304588A CH 675879 A5 CH675879 A5 CH 675879A5
- Authority
- CH
- Switzerland
- Prior art keywords
- acid
- peptide
- sulfide
- reduction
- concentration
- Prior art date
Links
- QMMFVYPAHWMCMS-UHFFFAOYSA-N Dimethyl sulfide Chemical group CSC QMMFVYPAHWMCMS-UHFFFAOYSA-N 0.000 claims description 60
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 claims description 55
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 53
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 32
- 238000000034 method Methods 0.000 claims description 27
- 230000009467 reduction Effects 0.000 claims description 23
- 239000002253 acid Substances 0.000 claims description 19
- 102000004169 proteins and genes Human genes 0.000 claims description 17
- 108090000623 proteins and genes Proteins 0.000 claims description 17
- 229910052736 halogen Inorganic materials 0.000 claims description 15
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 claims description 14
- UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 claims description 13
- 150000002367 halogens Chemical class 0.000 claims description 13
- 230000008569 process Effects 0.000 claims description 11
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 7
- 239000011541 reaction mixture Substances 0.000 claims description 7
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 4
- 229930182817 methionine Natural products 0.000 claims description 4
- BMYNFMYTOJXKLE-UHFFFAOYSA-N 3-azaniumyl-2-hydroxypropanoate Chemical compound NCC(O)C(O)=O BMYNFMYTOJXKLE-UHFFFAOYSA-N 0.000 claims description 3
- XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 claims description 3
- 229940071870 hydroiodic acid Drugs 0.000 claims description 3
- 125000000217 alkyl group Chemical group 0.000 claims description 2
- 125000004432 carbon atom Chemical group C* 0.000 claims description 2
- 239000012429 reaction media Substances 0.000 claims description 2
- 239000000243 solution Substances 0.000 description 17
- 235000018102 proteins Nutrition 0.000 description 13
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 12
- 238000006243 chemical reaction Methods 0.000 description 10
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 6
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 6
- 229910052757 nitrogen Inorganic materials 0.000 description 6
- 102000051325 Glucagon Human genes 0.000 description 5
- 108060003199 Glucagon Proteins 0.000 description 5
- 229960004666 glucagon Drugs 0.000 description 5
- 150000003568 thioethers Chemical class 0.000 description 5
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 4
- 238000007385 chemical modification Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 230000014759 maintenance of location Effects 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 238000013139 quantization Methods 0.000 description 4
- 150000003462 sulfoxides Chemical class 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- QEFRNWWLZKMPFJ-ZXPFJRLXSA-N L-methionine (R)-S-oxide Chemical compound C[S@@](=O)CC[C@H]([NH3+])C([O-])=O QEFRNWWLZKMPFJ-ZXPFJRLXSA-N 0.000 description 3
- QEFRNWWLZKMPFJ-YGVKFDHGSA-N L-methionine (R)-S-oxide group Chemical group N[C@@H](CCS(=O)C)C(=O)O QEFRNWWLZKMPFJ-YGVKFDHGSA-N 0.000 description 3
- QEFRNWWLZKMPFJ-UHFFFAOYSA-N L-methionine sulphoxide Natural products CS(=O)CCC(N)C(O)=O QEFRNWWLZKMPFJ-UHFFFAOYSA-N 0.000 description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 239000004254 Ammonium phosphate Substances 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- KRHYYFGTRYWZRS-UHFFFAOYSA-N Fluorane Chemical compound F KRHYYFGTRYWZRS-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 229910000148 ammonium phosphate Inorganic materials 0.000 description 2
- 235000019289 ammonium phosphates Nutrition 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- MNNHAPBLZZVQHP-UHFFFAOYSA-N diammonium hydrogen phosphate Chemical compound [NH4+].[NH4+].OP([O-])([O-])=O MNNHAPBLZZVQHP-UHFFFAOYSA-N 0.000 description 2
- LJSQFQKUNVCTIA-UHFFFAOYSA-N diethyl sulfide Chemical compound CCSCC LJSQFQKUNVCTIA-UHFFFAOYSA-N 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- QEWYKACRFQMRMB-UHFFFAOYSA-N fluoroacetic acid Chemical compound OC(=O)CF QEWYKACRFQMRMB-UHFFFAOYSA-N 0.000 description 2
- -1 halogen acids Chemical class 0.000 description 2
- IXCSERBJSXMMFS-UHFFFAOYSA-N hcl hcl Chemical compound Cl.Cl IXCSERBJSXMMFS-UHFFFAOYSA-N 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 2
- ITMCEJHCFYSIIV-UHFFFAOYSA-N triflic acid Chemical compound OS(=O)(=O)C(F)(F)F ITMCEJHCFYSIIV-UHFFFAOYSA-N 0.000 description 2
- LJCZNYWLQZZIOS-UHFFFAOYSA-N 2,2,2-trichlorethoxycarbonyl chloride Chemical compound ClC(=O)OCC(Cl)(Cl)Cl LJCZNYWLQZZIOS-UHFFFAOYSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- NOKPBJYHPHHWAN-REOHCLBHSA-N S-sulfo-L-cysteine Chemical compound OC(=O)[C@@H](N)CSS(O)(=O)=O NOKPBJYHPHHWAN-REOHCLBHSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- 239000003518 caustics Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 150000001945 cysteines Chemical class 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000001066 destructive effect Effects 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- LTYMSROWYAPPGB-UHFFFAOYSA-N diphenyl sulfide Chemical compound C=1C=CC=CC=1SC1=CC=CC=C1 LTYMSROWYAPPGB-UHFFFAOYSA-N 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 229910000041 hydrogen chloride Inorganic materials 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- IOPLHGOSNCJOOO-UHFFFAOYSA-N methyl 3,4-diaminobenzoate Chemical compound COC(=O)C1=CC=C(N)C(N)=C1 IOPLHGOSNCJOOO-UHFFFAOYSA-N 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- LXMSZDCAJNLERA-ZHYRCANASA-N spironolactone Chemical compound C([C@@H]1[C@]2(C)CC[C@@H]3[C@@]4(C)CCC(=O)C=C4C[C@H]([C@@H]13)SC(=O)C)C[C@@]21CCC(=O)O1 LXMSZDCAJNLERA-ZHYRCANASA-N 0.000 description 1
- ZERULLAPCVRMCO-UHFFFAOYSA-N sulfure de di n-propyle Natural products CCCSCCC ZERULLAPCVRMCO-UHFFFAOYSA-N 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 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 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
- C07K1/14—Extraction; Separation; Purification
-
- 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
- C07K1/06—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents
- C07K1/061—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using protecting groups
- C07K1/067—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using protecting groups for sulfur-containing functions
-
- 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
- C07K1/12—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by hydrolysis, i.e. solvolysis in general
- C07K1/122—Hydrolysis with acids different from HF
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/088,739 US4835254A (en) | 1987-08-24 | 1987-08-24 | Process for reducing methionine sulfoxide residues in peptides or proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CH675879A5 true CH675879A5 (ref) | 1990-11-15 |
Family
ID=22213162
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CH3045/88A CH675879A5 (ref) | 1987-08-24 | 1988-08-12 |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US4835254A (ref) |
| JP (1) | JPH02262590A (ref) |
| KR (1) | KR890003798A (ref) |
| CN (1) | CN1029976C (ref) |
| BE (1) | BE1004198A3 (ref) |
| CA (1) | CA1315482C (ref) |
| CH (1) | CH675879A5 (ref) |
| DE (1) | DE3828287A1 (ref) |
| DK (1) | DK465588A (ref) |
| FR (1) | FR2619820B1 (ref) |
| GB (1) | GB2209033B (ref) |
| HU (1) | HU200438B (ref) |
| IL (1) | IL87479A (ref) |
| IT (1) | IT1226864B (ref) |
| NL (1) | NL8802041A (ref) |
| SE (1) | SE503255C2 (ref) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2682061B2 (ja) * | 1988-10-07 | 1997-11-26 | 藤沢薬品工業株式会社 | ペプチドの分子内ジスルフィド結合の形成法 |
| US5272135A (en) * | 1991-03-01 | 1993-12-21 | Chiron Ophthalmics, Inc. | Method for the stabilization of methionine-containing polypeptides |
| GB2451441B (en) | 2007-07-30 | 2012-07-11 | Lein Applied Diagnostics Ltd | Optical alignment apparatus and method thereof |
| KR102650195B1 (ko) | 2020-11-11 | 2024-04-09 | 주식회사 제론메드 | 유리 메티오닌ｒ설폭사이드를 정량적으로 측정할 수 있는 형광단백질 센서 및 이의 용도 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4745178A (en) * | 1987-04-22 | 1988-05-17 | Eli Lilly And Company | Process for selective peptide bond cleavage using sulfoxides and CF3 CO |
-
1987
- 1987-08-24 US US07/088,739 patent/US4835254A/en not_active Expired - Lifetime
-
1988
- 1988-08-12 CH CH3045/88A patent/CH675879A5/de not_active IP Right Cessation
- 1988-08-16 CA CA000574821A patent/CA1315482C/en not_active Expired - Fee Related
- 1988-08-17 NL NL8802041A patent/NL8802041A/nl not_active Application Discontinuation
- 1988-08-17 IL IL87479A patent/IL87479A/xx not_active IP Right Cessation
- 1988-08-18 IT IT8821716A patent/IT1226864B/it active
- 1988-08-19 KR KR1019880010521A patent/KR890003798A/ko not_active Ceased
- 1988-08-19 DE DE3828287A patent/DE3828287A1/de not_active Withdrawn
- 1988-08-19 SE SE8802941A patent/SE503255C2/sv not_active IP Right Cessation
- 1988-08-19 DK DK465588A patent/DK465588A/da unknown
- 1988-08-22 BE BE8800956A patent/BE1004198A3/fr not_active IP Right Cessation
- 1988-08-22 FR FR8811081A patent/FR2619820B1/fr not_active Expired - Lifetime
- 1988-08-22 GB GB8819861A patent/GB2209033B/en not_active Expired - Lifetime
- 1988-08-22 CN CN88106236A patent/CN1029976C/zh not_active Expired - Fee Related
- 1988-08-23 JP JP63209319A patent/JPH02262590A/ja active Pending
- 1988-08-23 HU HU884435A patent/HU200438B/hu not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| IL87479A0 (en) | 1989-01-31 |
| DK465588A (da) | 1989-03-17 |
| IT8821716A0 (it) | 1988-08-18 |
| GB2209033B (en) | 1991-01-02 |
| US4835254A (en) | 1989-05-30 |
| SE503255C2 (sv) | 1996-04-29 |
| JPH02262590A (ja) | 1990-10-25 |
| NL8802041A (nl) | 1989-03-16 |
| GB2209033A (en) | 1989-04-26 |
| KR890003798A (ko) | 1989-04-18 |
| CN1031538A (zh) | 1989-03-08 |
| DE3828287A1 (de) | 1989-03-09 |
| DK465588D0 (da) | 1988-08-19 |
| IT1226864B (it) | 1991-02-20 |
| BE1004198A3 (fr) | 1992-10-13 |
| FR2619820B1 (fr) | 1992-11-13 |
| FR2619820A1 (fr) | 1989-03-03 |
| CA1315482C (en) | 1993-03-30 |
| HU200438B (en) | 1990-06-28 |
| CN1029976C (zh) | 1995-10-11 |
| GB8819861D0 (en) | 1988-09-21 |
| SE8802941L (sv) | 1989-02-25 |
| HUT48560A (en) | 1989-06-28 |
| SE8802941D0 (sv) | 1988-08-19 |
| IL87479A (en) | 1993-02-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DE60116137T2 (de) | Derivatisierung von proteinen in wässrigem lösungsmittel | |
| EP0305760B1 (de) | Verfahren zur Isolierung basischer Proteine aus Proteingemischen | |
| DE69029370T2 (de) | Erythropoietin-Isoformen | |
| DE19735711C2 (de) | Verfahren zur Herstellung eines Vorläufers von Insulin oder Insulinderivaten mit korrekt verbundenen Cystinbrücken | |
| DE4028120C2 (de) | Verfahren zur Reinigung von Insulin und/oder Insulinderivaten | |
| EP0393725A1 (de) | Verfahren zur Aktivierung von gentechnolgish hergestellten, heterologen, Disulfidbrücken aufweisenden eukaryontischen Proteinen nach Expression in Prokaryonten | |
| EP0354507B1 (de) | Verfahren zur Herstellung von Des-B30-Insulinen und Des-B30-Insulinderivaten | |
| DE3650276T2 (de) | Proteinreinigung. | |
| DE69636739T2 (de) | Verfahren zur rückfaltung von menschlichem activin a | |
| DE2917899A1 (de) | Lyophilisierte urokinasezubereitung zu injektionszwecken und verfahren zu ihrer herstellung | |
| DE68926153T2 (de) | Verfahren zum Lösen und Renaturieren von Somatotropin | |
| EP0241022A2 (de) | Verfahren zur Renaturierung von Proteinen | |
| CH675879A5 (ref) | ||
| DE1102973B (de) | Verfahren zur Herstellung von hoch gereinigten Kallikrein-Praeparaten | |
| DE69720693T2 (de) | Fsh und lh trennungs- und reinigungsverfahren | |
| DE69232097T2 (de) | C-terminale peptidsequenzierung unter verwendung von diphenylphosphoroisothiocyanidat und pyridin | |
| EP0245267B1 (de) | Verfahren zur gewinnung von insulin-vorläufern aus reaktionsgemischen, die bei der faltung von insulin-vorläufern aus den entsprechenden s-sulfonaten anfallen | |
| DE3016548C2 (de) | Herabsetzung der thermischen Stabilität von mikrobiellem Mucor-Rennin und dessen Verwendung zur Käsebereitung | |
| DE68908203T2 (de) | Spaltungsverfahren bei Methioninresten oder Polypeptiden. | |
| DD148298A5 (de) | Verfahren zur reinigung von insulin | |
| DD157612A5 (de) | Verfahren zur herstellung eines insulinvorlaeufers | |
| DE69013475T2 (de) | Methode zur Auflösung und Naturation von Somatotropin unter Verwendung von einer niedrigen Harnstoffkonzentration. | |
| DE3884660T2 (de) | Verfahren zur selektiven Spaltung der Peptidbindung. | |
| DE68913080T2 (de) | S-sulfonierte Calcitonin-Derivate. | |
| DE1468964C3 (de) | In Wasser sich rasch losende sulfatierte Kartoffelstarke Amylopektin schwefelsäureester und Verfahren zu ihrer Herstellung |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PL | Patent ceased |