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A large-scale purification of recombinant histone H1. 5 from Escherichia coli

Pyo, Sang-Hyun LU ; Lee, Jae-Hyun ; Park, Heung-Bok ; Hong, Seung-Suh and Kim, Jin-Hyun (2001) In Protein Expression and Purification 23(1). p.38-44
Abstract
An Escherichia coli expression system has been constructed for production of biologically active recombinant histone H1.5. A process of fermentation and purification method at a large scale has been developed. Recombinant histone H1.5 was released from the high density cultured cells by high-pressure homogenization. For an efficient removal of cell debris and partial purification of basic histone H1.5 in a single step, the whole cell lysates were directly loaded onto an expanded bed column packed with the strong cation exchanger (Streamline SP). Complete removal of various impurities was achieved by a combination of hydroxyapatite chromatography and the following cation exchange chromatography with high grade strong cation exchanger (POROS... (More)
An Escherichia coli expression system has been constructed for production of biologically active recombinant histone H1.5. A process of fermentation and purification method at a large scale has been developed. Recombinant histone H1.5 was released from the high density cultured cells by high-pressure homogenization. For an efficient removal of cell debris and partial purification of basic histone H1.5 in a single step, the whole cell lysates were directly loaded onto an expanded bed column packed with the strong cation exchanger (Streamline SP). Complete removal of various impurities was achieved by a combination of hydroxyapatite chromatography and the following cation exchange chromatography with high grade strong cation exchanger (POROS 20 HS), and finally endotoxins were removed by ultrafiltration using a 100-kDa cut-off membrane, which gave the level of endotoxin below 0.5 EU/mg. The … (Less)
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author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Protein Expression and Purification
volume
23
issue
1
pages
38 - 44
publisher
Academic Press
ISSN
1046-5928
DOI
10.1006/prep.2001.1471
language
English
LU publication?
no
id
1f03f840-e5d7-4bda-bf16-dd7de8f9e05b
date added to LUP
2025-09-05 17:51:35
date last changed
2025-09-17 12:26:59
@article{1f03f840-e5d7-4bda-bf16-dd7de8f9e05b,
  abstract     = {{An Escherichia coli expression system has been constructed for production of biologically active recombinant histone H1.5. A process of fermentation and purification method at a large scale has been developed. Recombinant histone H1.5 was released from the high density cultured cells by high-pressure homogenization. For an efficient removal of cell debris and partial purification of basic histone H1.5 in a single step, the whole cell lysates were directly loaded onto an expanded bed column packed with the strong cation exchanger (Streamline SP). Complete removal of various impurities was achieved by a combination of hydroxyapatite chromatography and the following cation exchange chromatography with high grade strong cation exchanger (POROS 20 HS), and finally endotoxins were removed by ultrafiltration using a 100-kDa cut-off membrane, which gave the level of endotoxin below 0.5 EU/mg. The …}},
  author       = {{Pyo, Sang-Hyun and Lee, Jae-Hyun and Park, Heung-Bok and Hong, Seung-Suh and Kim, Jin-Hyun}},
  issn         = {{1046-5928}},
  language     = {{eng}},
  month        = {{10}},
  number       = {{1}},
  pages        = {{38--44}},
  publisher    = {{Academic Press}},
  series       = {{Protein Expression and Purification}},
  title        = {{A large-scale purification of recombinant histone H1. 5 from <i>Escherichia coli</i>}},
  url          = {{http://dx.doi.org/10.1006/prep.2001.1471}},
  doi          = {{10.1006/prep.2001.1471}},
  volume       = {{23}},
  year         = {{2001}},
}