CN1470634A - Enterpeptidase light chain variant with high activity and high stability - Google Patents
Enterpeptidase light chain variant with high activity and high stability Download PDFInfo
- Publication number
- CN1470634A CN1470634A CNA021380171A CN02138017A CN1470634A CN 1470634 A CN1470634 A CN 1470634A CN A021380171 A CNA021380171 A CN A021380171A CN 02138017 A CN02138017 A CN 02138017A CN 1470634 A CN1470634 A CN 1470634A
- Authority
- CN
- China
- Prior art keywords
- light chain
- enterpeptidase light
- enterpeptidase
- chain variant
- wild
- 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
- 230000000694 effects Effects 0.000 title abstract description 21
- 108010013369 Enteropeptidase Proteins 0.000 claims abstract description 29
- 102100029727 Enteropeptidase Human genes 0.000 claims abstract description 29
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 21
- 102000004190 Enzymes Human genes 0.000 claims abstract description 14
- 108090000790 Enzymes Proteins 0.000 claims abstract description 14
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 10
- 235000018102 proteins Nutrition 0.000 claims abstract description 8
- 230000035772 mutation Effects 0.000 claims abstract description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 23
- 238000002360 preparation method Methods 0.000 claims description 16
- 238000002703 mutagenesis Methods 0.000 claims description 6
- 231100000350 mutagenesis Toxicity 0.000 claims description 6
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 5
- 230000009257 reactivity Effects 0.000 claims description 5
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 4
- 230000008859 change Effects 0.000 claims description 3
- 238000012407 engineering method Methods 0.000 claims description 2
- 229920002684 Sepharose Polymers 0.000 abstract description 10
- 238000001042 affinity chromatography Methods 0.000 abstract description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 abstract 1
- 235000018417 cysteine Nutrition 0.000 abstract 1
- 241000894006 Bacteria Species 0.000 description 19
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 230000004927 fusion Effects 0.000 description 16
- 239000000047 product Substances 0.000 description 12
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 11
- 230000009182 swimming Effects 0.000 description 9
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 238000013016 damping Methods 0.000 description 7
- 239000012530 fluid Substances 0.000 description 7
- 239000007788 liquid Substances 0.000 description 7
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 238000012408 PCR amplification Methods 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 230000000968 intestinal effect Effects 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 5
- 238000000855 fermentation Methods 0.000 description 5
- 230000004151 fermentation Effects 0.000 description 5
- FRXSZNDVFUDTIR-UHFFFAOYSA-N 6-methoxy-1,2,3,4-tetrahydroquinoline Chemical compound N1CCCC2=CC(OC)=CC=C21 FRXSZNDVFUDTIR-UHFFFAOYSA-N 0.000 description 4
- 101800000407 Brain natriuretic peptide 32 Proteins 0.000 description 4
- 102400000667 Brain natriuretic peptide 32 Human genes 0.000 description 4
- 101800002247 Brain natriuretic peptide 45 Proteins 0.000 description 4
- 239000006142 Luria-Bertani Agar Substances 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 150000002460 imidazoles Chemical class 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 239000007853 buffer solution Substances 0.000 description 3
- 239000004202 carbamide Substances 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 239000012149 elution buffer Substances 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 238000009413 insulation Methods 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- SEQKRHFRPICQDD-UHFFFAOYSA-N N-tris(hydroxymethyl)methylglycine Chemical compound OCC(CO)(CO)[NH2+]CC([O-])=O SEQKRHFRPICQDD-UHFFFAOYSA-N 0.000 description 2
- 108020001621 Natriuretic Peptide Proteins 0.000 description 2
- 102000004571 Natriuretic peptide Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- 108020005038 Terminator Codon Proteins 0.000 description 2
- 102100036407 Thioredoxin Human genes 0.000 description 2
- 108010084455 Zeocin Proteins 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- KLOHDWPABZXLGI-YWUHCJSESA-M ampicillin sodium Chemical compound [Na+].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 KLOHDWPABZXLGI-YWUHCJSESA-M 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 230000004087 circulation Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 210000001198 duodenum Anatomy 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000000692 natriuretic peptide Substances 0.000 description 2
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000004153 renaturation Methods 0.000 description 2
- 238000003757 reverse transcription PCR Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 108060008226 thioredoxin Proteins 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 101500026735 Homo sapiens Brain natriuretic peptide 32 Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
- UZMAPBJVXOGOFT-UHFFFAOYSA-N Syringetin Natural products COC1=C(O)C(OC)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UZMAPBJVXOGOFT-UHFFFAOYSA-N 0.000 description 1
- 239000007997 Tricine buffer Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- KCFYHBSOLOXZIF-UHFFFAOYSA-N dihydrochrysin Natural products COC1=C(O)C(OC)=CC(C2OC3=CC(O)=CC(O)=C3C(=O)C2)=C1 KCFYHBSOLOXZIF-UHFFFAOYSA-N 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 235000003969 glutathione Nutrition 0.000 description 1
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 239000003161 ribonuclease inhibitor Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 108010066925 sleep-promoting factor B Proteins 0.000 description 1
- HLBBKKJFGFRGMU-UHFFFAOYSA-M sodium formate Chemical compound [Na+].[O-]C=O HLBBKKJFGFRGMU-UHFFFAOYSA-M 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229910000406 trisodium phosphate Inorganic materials 0.000 description 1
- 235000019801 trisodium phosphate Nutrition 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000029534 trypsinogen activation Effects 0.000 description 1
Images
Landscapes
- Enzymes And Modification Thereof (AREA)
Abstract
Description
Claims (3)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN 02138017 CN1214107C (en) | 2002-07-26 | 2002-07-26 | Enterpeptidase light chain variant with high activity and high stability |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN 02138017 CN1214107C (en) | 2002-07-26 | 2002-07-26 | Enterpeptidase light chain variant with high activity and high stability |
Publications (2)
Publication Number | Publication Date |
---|---|
CN1470634A true CN1470634A (en) | 2004-01-28 |
CN1214107C CN1214107C (en) | 2005-08-10 |
Family
ID=34147123
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN 02138017 Expired - Fee Related CN1214107C (en) | 2002-07-26 | 2002-07-26 | Enterpeptidase light chain variant with high activity and high stability |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN1214107C (en) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101624588B (en) * | 2007-05-11 | 2012-02-22 | 上海抗体药物国家工程研究中心有限公司 | Light chain mutant of recombination cattle enterokinase |
WO2013092855A1 (en) * | 2011-12-23 | 2013-06-27 | Novo Nordisk A/S | Modified enterokinase light chain |
CN103998606A (en) * | 2011-12-23 | 2014-08-20 | 诺沃—诺迪斯克有限公司 | Modified enterokinase light chain |
CN104911166A (en) * | 2014-12-15 | 2015-09-16 | 上海张江生物技术有限公司 | Novel recombinant medaka enteropeptidase light chain protein |
-
2002
- 2002-07-26 CN CN 02138017 patent/CN1214107C/en not_active Expired - Fee Related
Cited By (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101624588B (en) * | 2007-05-11 | 2012-02-22 | 上海抗体药物国家工程研究中心有限公司 | Light chain mutant of recombination cattle enterokinase |
WO2013092855A1 (en) * | 2011-12-23 | 2013-06-27 | Novo Nordisk A/S | Modified enterokinase light chain |
CN103998606A (en) * | 2011-12-23 | 2014-08-20 | 诺沃—诺迪斯克有限公司 | Modified enterokinase light chain |
JP2015502167A (en) * | 2011-12-23 | 2015-01-22 | ノヴォ ノルディスク アー/エス | Modified enterokinase light chain |
US9611466B2 (en) | 2011-12-23 | 2017-04-04 | Novo Nordisk A/S | Modified enterokinase light chain |
CN103998606B (en) * | 2011-12-23 | 2018-04-17 | 诺沃—诺迪斯克有限公司 | The Enterpeptidase light chain of modification |
CN104911166A (en) * | 2014-12-15 | 2015-09-16 | 上海张江生物技术有限公司 | Novel recombinant medaka enteropeptidase light chain protein |
Also Published As
Publication number | Publication date |
---|---|
CN1214107C (en) | 2005-08-10 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN100347189C (en) | High-level composing production for anthrax protection antigen | |
CN102994601B (en) | Method for preparing collagen small peptide by utilizing marine collagenase MCP-01 | |
CN1189565C (en) | Efficient prokaryotic expression carrier | |
CN1214107C (en) | Enterpeptidase light chain variant with high activity and high stability | |
CN110777140B (en) | Chondrosulphatase AC mutant and preparation method thereof | |
CN113637663B (en) | Trypsin mutant with improved heat stability | |
CN1670033A (en) | Method for preparing human interleukin 29 and recombinant IL-29 engineering strain | |
CN101555485B (en) | Non-fusion expression of recombinant human parathyroid hormone (1-84) and large-scale preparation method | |
CN87102497A (en) | Alpha interferon analogue | |
CN101045923B (en) | Process of producing interleukin analog | |
CN1401662A (en) | Anticoagulation and thrombolytic thrombus target fusion mA5UKB | |
CN1093175C (en) | New structured L-asparaginase engineering bacterium and its production culture | |
CN1164749C (en) | Cattle enteropeptidase catalyzing subunit gene and its gene engineering production process | |
CN1098742A (en) | Aminopeptidase and this enzyme and its proteic preparation method | |
CN1177051C (en) | Recombinant thymin alpha-1 and its prepn | |
CN1408863A (en) | Human interleukin-10 gene sequenc and E coli containing the said gene sequence | |
CN102585013B (en) | Fusion protein containing omega interferon and method for preparing same | |
CN1194015C (en) | Effective renaturation liquid of recombinant human interon inclusion body and renaturation method | |
CN1274823C (en) | Production of human interleukin 288 and recombined IL-288 engineering bacteria | |
CN1693458A (en) | Production method of human interleukin 28 A and recombination IL-28A engineering bacteria | |
CN114107260B (en) | Fucoidan sulfate degrading enzyme OUC-FaFcn1 and application thereof | |
CN1940065A (en) | Oriented mutant gene engineering barr kinase and its use | |
CN1616488A (en) | Primary structure of Anjikang protein of snake soure desintegration mutant anti-tumor medicine | |
CN1990861A (en) | Preparation method of active carboxypeptidase B | |
CN1966690A (en) | Prokaryotic expression plasmid vector pKpL5 for use in genetic engineering production an its construction |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
C14 | Grant of patent or utility model | ||
GR01 | Patent grant | ||
ASS | Succession or assignment of patent right |
Owner name: SUZHOU LANDING BIOPHARMACEUTICAL CO., LTD. Free format text: FORMER OWNER: LIU JIANNING Effective date: 20110930 |
|
C41 | Transfer of patent application or patent right or utility model | ||
COR | Change of bibliographic data |
Free format text: CORRECT: ADDRESS; FROM: 215000 SUZHOU, JIANGSU PROVINCE TO: 215028 SUZHOU, JIANGSU PROVINCE |
|
TR01 | Transfer of patent right |
Effective date of registration: 20110930 Address after: 215028 No. 118 Longtan Road, Suzhou Industrial Park, Jiangsu Patentee after: SUZHOU LANDING BIOPHARMACEUTICAL CO., LTD. Address before: 215000, Jiangsu, Suzhou Province Home Lane Lane 1, Room 203 Patentee before: Liu Jianning |
|
CF01 | Termination of patent right due to non-payment of annual fee | ||
CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20050810 Termination date: 20190726 |