Renaturation of recombinant human neurotrophin‐3 from inclusion bodies using a suppressor agent of aggregation

@article{Suenaga1998RenaturationOR,  title={Renaturation of recombinant human neurotrophin‐3 from inclusion bodies using a suppressor agent of aggregation},  author={Masato Suenaga and Hiroaki Ohmae and Shinji Tsuji and Takashi Itoh and Osamu Nishimura},  journal={Biotechnology and Applied Biochemistry},  year={1998},  volume={28},  url={https://api.semanticscholar.org/CorpusID:45466609}}
The refolding process using the aggregation suppressor L‐arginine in the renaturation of neurotrophin‐3 was applied, and biologically active neurotrophine 3 was obtained at high yield from the inclusion bodies.

48 Citations

OPTIMIZING PRIMARY RECOVERY AND REFOLDING OF HUMAN INTERFERON-β FROM ESCHERICHIA COLI INCLUSION BODIES

The best recovery of inclusion bodies was found at a concentration 0.5 M of Triton X-100, themaximum efficiency of solubility was found in pH 10.5 and the maximum efficiency of refolding was achieved by final buffer containing 2M urea and 0.6 M L-Arg.

Optimized procedure for renaturation of recombinant human bone morphogenetic protein‐2 at high protein concentration

The aggregation suppressor 2‐(cyclohexylamino)ethanesulfonic acid (CHES) proved to be superior with respect to the final renaturation yield, although, in comparison to the more common arginine, it was less efficient in preventing aggregation of rhBMP‐2 during refolding.

L-arginine mediated renaturation enhances yield of human, α6 Type IV collagen non-collagenous domain from bacterial inclusion bodies.

Direct stirring and on-column renaturation methods using L-arginine and different size exclusion chromatography matrices were applied for enhancing the solubility in purifying the recombinant α6(IV)NC1 from bacterial inclusion bodies, which enabled purification of higher quantities of soluble protein from inclusion bodies.

l-Arginine Suppresses Aggregation of Recombinant Growth Hormones in Refolding Process from E. coli Inclusion Bodies

l-Arginine effectively suppressed the precipitation of growth hormones during dilution, but did not inhibit soluble oligomers formation in mink and porcine growth hormones purification from 4 g of biomass.

Refolding Technology for scFv Using a New Detergent, N-Lauroyl-L-glutamate and Arginine

A novel refolding system using a new amino acid-based detergent, N-lauroyl-L-glutamate, and arginine is described, which appears to readily dissociate from proteins below critical micelle concentration (CMC), while remaining effective in protein solubilization above CMC.

Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli.

The recombinant prepro-form of human matrix metalloproteinase 7 (matrilysin or MMP-7) was overexpressed in Escherichia coli as insoluble inclusion bodies and was refolded by 100-fold dilution after solubilization with 6 M guanidine HCl.

11 References

Size and Density of Protein Inclusion Bodies

Sedimentation studies indicated that the density of the protein inclusion bodies increases with thedensity of the suspending solvent, which is consistent with the bodies having a voidage and accessible to the suspending fluid of 70% and 85% of the total volume.

New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor

The crystal structure of the murine NGF dimer is reported, which reveals a novel protomer structure consisting of three antiparallel pairs of β strands, together forming a flat surface that provides a model for rational design of analogues of NGF and its relatives and for testing the NGF-receptor recognition determinants critical for signal transduction.

Identification and characterization of a novel member of the nerve growth factor/brain-derived neurotrophic factor family

Taking advantage of sequence identities between NGF and BDNF, a third member of this family of secretory proteins is identified, which is named neurotrophin-3, and a remarkable number of amino acid identities are revealed, including all cys-teine residues.

Neurotrophin-3: a neurotrophic factor related to NGF and BDNF.

The distribution of NT-3 messenger RNA and its biological activity on a variety of neuronal populations clearly distinguishNT-3 from NGF and BDNF, and provide compelling evidence that NT- 3 is an authentic neurotrophic factor that has its own characteristic role in vivo.

Molecular characterization of recombinant human acidic fibroblast growth factor produced in E. coli: comparative studies with human basic fibroblast growth factor.

Results implied that haFGF was potentiated by heparin and that this potentiation did not involve a significant change in the conformation of the haF GF molecule.

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major…

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