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Composite imprinted macroporous hydrogels for haemoglobin purification from cell homogenate

Hajizadeh, Solmaz LU orcid ; Kettisen, Karin LU ; Gram, Magnus LU orcid ; Bülow, Leif LU and Ye, Lei LU orcid (2018) In Journal of Chromatography A 1534. p.22-31
Abstract

Purification of haemoglobin (Hb) has been studied for many years due to its ability to act as an oxygen carrier and its possible use in urgent clinical treatment. In this study, different types of chromatography columns were developed for Hb purification. Two of them showed satisfactory results as affinity chromatography columns and were thus studied more extensively. The affinity adsorbents were prepared by molecular imprinting techniques. In the first case, Pickering emulsion polymerization was used to prepare affinity adsorbents based on molecular imprinting technology. The imprinted particles were immobilized via covalent bonds on the surface of cryogel, a macroporous hydrogel produced by free radical polymerization under sub-zero... (More)

Purification of haemoglobin (Hb) has been studied for many years due to its ability to act as an oxygen carrier and its possible use in urgent clinical treatment. In this study, different types of chromatography columns were developed for Hb purification. Two of them showed satisfactory results as affinity chromatography columns and were thus studied more extensively. The affinity adsorbents were prepared by molecular imprinting techniques. In the first case, Pickering emulsion polymerization was used to prepare affinity adsorbents based on molecular imprinting technology. The imprinted particles were immobilized via covalent bonds on the surface of cryogel, a macroporous hydrogel produced by free radical polymerization under sub-zero temperature. In the second case, the affinity sites for Hb were formed directly on an acrylamide cryogel by protein imprinting during the cryogelation. The dynamic binding capacity of the composite cryogel with the immobilized particles and the directly imprinted acrylamide cryogel was found to be 5.2 mg/g and 3.6 mg/g, respectively. The affinity columns showed high selectivity towards Hb in spite of the presence of serum albumin as well as other interfering substances in non-clarified cell homogenates. The maximum capacity in batch mode, the fluid flow and other physical and chemical properties of these columns were investigated.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Affinity chromatography, Composite cryogel, Haemoglobin purification, Molecularly imprinting polymer, Pickering emulsion polymerization
in
Journal of Chromatography A
volume
1534
pages
22 - 31
publisher
Elsevier
external identifiers
  • scopus:85039148040
  • pmid:29289339
ISSN
0021-9673
DOI
10.1016/j.chroma.2017.12.038
language
English
LU publication?
yes
id
0e76ba3b-5c2c-4dec-8342-1dfca7b80f51
date added to LUP
2018-01-08 13:23:34
date last changed
2024-03-31 22:12:20
@article{0e76ba3b-5c2c-4dec-8342-1dfca7b80f51,
  abstract     = {{<p>Purification of haemoglobin (Hb) has been studied for many years due to its ability to act as an oxygen carrier and its possible use in urgent clinical treatment. In this study, different types of chromatography columns were developed for Hb purification. Two of them showed satisfactory results as affinity chromatography columns and were thus studied more extensively. The affinity adsorbents were prepared by molecular imprinting techniques. In the first case, Pickering emulsion polymerization was used to prepare affinity adsorbents based on molecular imprinting technology. The imprinted particles were immobilized via covalent bonds on the surface of cryogel, a macroporous hydrogel produced by free radical polymerization under sub-zero temperature. In the second case, the affinity sites for Hb were formed directly on an acrylamide cryogel by protein imprinting during the cryogelation. The dynamic binding capacity of the composite cryogel with the immobilized particles and the directly imprinted acrylamide cryogel was found to be 5.2 mg/g and 3.6 mg/g, respectively. The affinity columns showed high selectivity towards Hb in spite of the presence of serum albumin as well as other interfering substances in non-clarified cell homogenates. The maximum capacity in batch mode, the fluid flow and other physical and chemical properties of these columns were investigated.</p>}},
  author       = {{Hajizadeh, Solmaz and Kettisen, Karin and Gram, Magnus and Bülow, Leif and Ye, Lei}},
  issn         = {{0021-9673}},
  keywords     = {{Affinity chromatography; Composite cryogel; Haemoglobin purification; Molecularly imprinting polymer; Pickering emulsion polymerization}},
  language     = {{eng}},
  pages        = {{22--31}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Chromatography A}},
  title        = {{Composite imprinted macroporous hydrogels for haemoglobin purification from cell homogenate}},
  url          = {{http://dx.doi.org/10.1016/j.chroma.2017.12.038}},
  doi          = {{10.1016/j.chroma.2017.12.038}},
  volume       = {{1534}},
  year         = {{2018}},
}