Sijwali et al., 2001 - Google Patents
Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2Sijwali et al., 2001
- Document ID
- 15995778405031925521
- Author
- Sijwali P
- Brinen L
- Rosenthal P
- Publication year
- Publication venue
- Protein expression and purification
External Links
Snippet
The Plasmodium falciparum cysteine protease falcipain-2 is a potential new target for antimalarial chemotherapy. In order to obtain large quantities of active falcipain-2 for biochemical and structural analysis, a systematic assessment of optimal parameters for the …
- 108010017232 falcipain 2 0 title abstract description 62
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
-
- 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
- C07K1/1136—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 reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
-
- 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
- C07K1/1072—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 by covalent attachment of residues or functional groups
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K14/245—Escherichia (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2299/00—Coordinates from 3D structures of peptides, e.g. proteins or enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Sijwali et al. | Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2 | |
Singh et al. | Solubilization and refolding of bacterial inclusion body proteins | |
Maskos et al. | DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo | |
Clark | Protein refolding for industrial processes | |
JP5275306B2 (en) | Method for obtaining active β-NGF | |
EP2672984B1 (en) | Novel prongf mutants and uses thereof in the production of beta-ngf | |
EP3564376B1 (en) | Gene encoding alanyl-glutamine dipeptide biosynthetic enzyme and application thereof | |
Menzella et al. | High recovery of prochymosin from inclusion bodies using controlled air oxidation | |
Premkumar et al. | An unusual halotolerant α-type carbonic anhydrase from the alga Dunaliella salina functionally expressed in Escherichia coli | |
Gautam et al. | Non-chromatographic strategies for protein refolding | |
JP4239412B2 (en) | Method for producing transglutaminase | |
Vinogradov et al. | Solubilization and refolding of inclusion body proteins in reverse micelles | |
Hohenblum et al. | Bacterial expression and refolding of human trypsinogen | |
Mousavi et al. | Purification and efficient refolding process for recombinant tissue-type plasminogen activator derivative (reteplase) using glycerol and Tranexamic acid | |
Chitpinityol et al. | Site-specific mutations of calf chymosin B which influence milk-clotting activity | |
Babu et al. | Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli | |
Fazeli et al. | Effect of parallel feeding of oxidizing agent and protein on fed-batch refolding process of recombinant interferon beta-1b | |
Kim et al. | Refolding of Bacillus macerans cyclodextrin glucanotransferase expressed as inclusion bodies in recombinant Escherichia coli | |
Pérez-Sánchez et al. | High-level production of a recombinant Vibrio proteolyticus leucine aminopeptidase and its use for N-terminal methionine excision from interferon alpha-2b | |
JP5830524B2 (en) | Method for producing folded prethrombin or a derivative thereof | |
RU2697375C2 (en) | Plasmid vector prh15a for producing methionine-free interferon alpha-2b, bacterial strain escherichia coli bl21 de3 - producer of methionine-free interferon alpha-2b and method for producing methionine-free interferon alpha-2b | |
Rani et al. | Bioprocessing of inclusion bodies from E. coli. to prosduce bioactive recombinant proteins | |
EP3221448B1 (en) | Process for producing recombinant trypsin | |
MIRNAJD et al. | Optimizing refolding condition for recombinant tissue plasminogen activator | |
Nohara et al. | High performance in refolding of Streptomyces griseus trypsin by the aid of a mutant of Streptomyces subtilisin inhibitor designed as trypsin inhibitor |