A novel approach to monoclonal antibody separation using high performance liquid affinity chromatography (HPLAC) with SelectiSpher-10 protein G
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1104174
- author
- Ohlson, Sten ; Nilsson, Rune LU ; Niss, Ulf ; Kjellberg, Britt-Marie and Freiburghaus, Christian LU
- publishing date
- 1988
- 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}}, }