Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1475-2859
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli ; volume:13 ; number:1 ; day:12 ; month:9 ; year:2014 ; pages:1-14 ; date:12.2014
Microbial cell factories ; 13, Heft 1 (12.9.2014), 1-14, 12.2014
- Creator
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Castellanos-Mendoza, Andrea
- Contributor
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Castro-Acosta, Ricardo M.
Olvera, Alejandro
Zavala, Guadalupe
Mendoza-Vera, Miguel
García-Hernández, Enrique
Alagón, Alejandro
Trujillo-Roldán, Mauricio A.
Valdez-Cruz, Norma A.
SpringerLink (Online service)
- DOI
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10.1186/s12934-014-0137-9
- URN
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urn:nbn:de:1111-201607262569
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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2025-08-14T11:03:01+0200
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Castellanos-Mendoza, Andrea
- Castro-Acosta, Ricardo M.
- Olvera, Alejandro
- Zavala, Guadalupe
- Mendoza-Vera, Miguel
- García-Hernández, Enrique
- Alagón, Alejandro
- Trujillo-Roldán, Mauricio A.
- Valdez-Cruz, Norma A.
- SpringerLink (Online service)
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Impacts of oscillating cultivation conditions on the quality of recombinant inclusion bodies in Escherichia coli
Microwave assisted solubilization of inclusion bodies
Scalable production of recombinant three-finger proteins: from inclusion bodies to high quality molecular probes
One-step heating strategy for efficient solubilization of recombinant spider silk protein from inclusion bodies
Downstream processing of recombinant human insulin and its analogues production from E. coli inclusion bodies
Isolation of cell-free bacterial inclusion bodies
Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells
Quality control of inclusion bodies in Escherichia coli
Tailoring the properties of (catalytically)-active inclusion bodies
Conversion of recombinant human ferritin light chain inclusion bodies into uniform nanoparticles in Escherichia coli for facile production
Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies
Performance of beta-galactosidase inclusion bodies in enzymatic bioprocesses
Impacts of oscillating cultivation conditions on the quality of recombinant inclusion bodies in Escherichia coli
Microwave assisted solubilization of inclusion bodies
Scalable production of recombinant three-finger proteins: from inclusion bodies to high quality molecular probes
One-step heating strategy for efficient solubilization of recombinant spider silk protein from inclusion bodies
Downstream processing of recombinant human insulin and its analogues production from E. coli inclusion bodies
Isolation of cell-free bacterial inclusion bodies
Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells
Quality control of inclusion bodies in Escherichia coli
Tailoring the properties of (catalytically)-active inclusion bodies
Conversion of recombinant human ferritin light chain inclusion bodies into uniform nanoparticles in Escherichia coli for facile production
Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies