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A novel approach to monoclonal antibody separation using high performance liquid affinity chromatography (HPLAC) with SelectiSpher-10 protein G

Ohlson, Sten ; Nilsson, Rune LU ; Niss, Ulf ; Kjellberg, Britt-Marie and Freiburghaus, Christian LU (1988) In Journal of Immunological Methods 114(1-2). p.175-180
Abstract
Protein G, a bacterial cell wall protein extracted from strains of Streptococci, has been employed as a ligand in high performance liquid affinity chromatography (HPLAC) for separation of monoclonal antibodies. Examples are given of rapid high-resolution separations of rat and mouse monoclonal antibodies belonging to various subclasses. In comparison with protein A chromatography, we were able to show superior binding characteristics for SelectiSpher-10 protein G columns under conditions of 'low' ionic strength (about 0.1 M) and neutral pH (pH approximately 7). The monoclonal antibodies were isolated in high purity (greater than 90%) and with good recovery of specific activity (80-100%). We believe that the HPLAC technology based on... (More)
Protein G, a bacterial cell wall protein extracted from strains of Streptococci, has been employed as a ligand in high performance liquid affinity chromatography (HPLAC) for separation of monoclonal antibodies. Examples are given of rapid high-resolution separations of rat and mouse monoclonal antibodies belonging to various subclasses. In comparison with protein A chromatography, we were able to show superior binding characteristics for SelectiSpher-10 protein G columns under conditions of 'low' ionic strength (about 0.1 M) and neutral pH (pH approximately 7). The monoclonal antibodies were isolated in high purity (greater than 90%) and with good recovery of specific activity (80-100%). We believe that the HPLAC technology based on SelectiSpher-10 protein G is of potential value in the analysis and purification of monoclonal antibodies from various species and subclasses. (Less)
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author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Chromatography, Monoclonal antibody, high performance liquid affinity, Protein G
in
Journal of Immunological Methods
volume
114
issue
1-2
pages
175 - 180
publisher
Elsevier
external identifiers
  • pmid:3183389
  • scopus:0023734619
ISSN
1872-7905
DOI
10.1016/0022-1759(88)90170-6
language
English
LU publication?
no
id
a2afc5da-4912-40ff-b8db-09f83a0fb7ea (old id 1104174)
date added to LUP
2016-04-01 16:12:22
date last changed
2021-02-14 03:48:42
@article{a2afc5da-4912-40ff-b8db-09f83a0fb7ea,
  abstract     = {{Protein G, a bacterial cell wall protein extracted from strains of Streptococci, has been employed as a ligand in high performance liquid affinity chromatography (HPLAC) for separation of monoclonal antibodies. Examples are given of rapid high-resolution separations of rat and mouse monoclonal antibodies belonging to various subclasses. In comparison with protein A chromatography, we were able to show superior binding characteristics for SelectiSpher-10 protein G columns under conditions of 'low' ionic strength (about 0.1 M) and neutral pH (pH approximately 7). The monoclonal antibodies were isolated in high purity (greater than 90%) and with good recovery of specific activity (80-100%). We believe that the HPLAC technology based on SelectiSpher-10 protein G is of potential value in the analysis and purification of monoclonal antibodies from various species and subclasses.}},
  author       = {{Ohlson, Sten and Nilsson, Rune and Niss, Ulf and Kjellberg, Britt-Marie and Freiburghaus, Christian}},
  issn         = {{1872-7905}},
  keywords     = {{Chromatography; Monoclonal antibody; high performance liquid affinity; Protein G}},
  language     = {{eng}},
  number       = {{1-2}},
  pages        = {{175--180}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Immunological Methods}},
  title        = {{A novel approach to monoclonal antibody separation using high performance liquid affinity chromatography (HPLAC) with SelectiSpher-10 protein G}},
  url          = {{http://dx.doi.org/10.1016/0022-1759(88)90170-6}},
  doi          = {{10.1016/0022-1759(88)90170-6}},
  volume       = {{114}},
  year         = {{1988}},
}