Characterization of protein-protein interactions in recombinant hemoglobin producing escherichia coli cells using molecularly imprinted polymers
(2017) In Advances in Experimental Medicine and Biology 977. p.367-373- Abstract
The worldwide blood shortage has generated demands for alternatives to transfusible human blood. One such important option is based on recombinant hemoglobin-based oxygen carriers (rHBOCs). Most efforts have been focused on various E. coli based production systems. One of the key challenges in these systems is to devise an efficient and economical protein production strategy involving selection of suitable host cell and Hb variant, growth conditions and media engineering. Hb also influences the heterologous host cell metabolism and therefore the identification of modified protein-protein interactions is critical for optimizing Hb production. In this study, molecularly imprinted polymers (MIPs) directed against Hb were used to identify... (More)
The worldwide blood shortage has generated demands for alternatives to transfusible human blood. One such important option is based on recombinant hemoglobin-based oxygen carriers (rHBOCs). Most efforts have been focused on various E. coli based production systems. One of the key challenges in these systems is to devise an efficient and economical protein production strategy involving selection of suitable host cell and Hb variant, growth conditions and media engineering. Hb also influences the heterologous host cell metabolism and therefore the identification of modified protein-protein interactions is critical for optimizing Hb production. In this study, molecularly imprinted polymers (MIPs) directed against Hb were used to identify the human Hb protein interaction network in E. coli. One E. coli host protein, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), interacted strongly with Hb, especially fetal Hb (HbF).
(Less)
- author
- Zhang, Ka
LU
; Zhou, Tongchang
LU
; Ye, Lei
LU
and Bülow, Leif LU
- organization
- publishing date
- 2017
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Escherichia coli, Glyceraldehyde 3-phosphate dehydrogenase, Molecularly imprinted polymer, Protein-protein interaction, Recombinant hemoglobin
- in
- Advances in Experimental Medicine and Biology
- volume
- 977
- pages
- 7 pages
- publisher
- Springer
- external identifiers
-
- scopus:85026364612
- pmid:28685467
- ISSN
- 0065-2598
- DOI
- 10.1007/978-3-319-55231-6_48
- language
- English
- LU publication?
- yes
- id
- f82a9f76-dd79-46a1-9c20-973f4a08ed3f
- date added to LUP
- 2017-08-31 14:37:37
- date last changed
- 2025-01-07 19:44:35
@article{f82a9f76-dd79-46a1-9c20-973f4a08ed3f, abstract = {{<p>The worldwide blood shortage has generated demands for alternatives to transfusible human blood. One such important option is based on recombinant hemoglobin-based oxygen carriers (rHBOCs). Most efforts have been focused on various E. coli based production systems. One of the key challenges in these systems is to devise an efficient and economical protein production strategy involving selection of suitable host cell and Hb variant, growth conditions and media engineering. Hb also influences the heterologous host cell metabolism and therefore the identification of modified protein-protein interactions is critical for optimizing Hb production. In this study, molecularly imprinted polymers (MIPs) directed against Hb were used to identify the human Hb protein interaction network in E. coli. One E. coli host protein, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), interacted strongly with Hb, especially fetal Hb (HbF).</p>}}, author = {{Zhang, Ka and Zhou, Tongchang and Ye, Lei and Bülow, Leif}}, issn = {{0065-2598}}, keywords = {{Escherichia coli; Glyceraldehyde 3-phosphate dehydrogenase; Molecularly imprinted polymer; Protein-protein interaction; Recombinant hemoglobin}}, language = {{eng}}, pages = {{367--373}}, publisher = {{Springer}}, series = {{Advances in Experimental Medicine and Biology}}, title = {{Characterization of protein-protein interactions in recombinant hemoglobin producing <i>escherichia coli</i> cells using molecularly imprinted polymers}}, url = {{http://dx.doi.org/10.1007/978-3-319-55231-6_48}}, doi = {{10.1007/978-3-319-55231-6_48}}, volume = {{977}}, year = {{2017}}, }