Fractionation of rat IgG subclasses and screening for IgG Fc-binding to bacteria
(1982) In Molecular Immunology 19(1). p.119-126- Abstract
- The four IgG subclasses of the rat, IgGl, IgG2a, IgG2b and IgG2c, were purified from normal serum by a combination of protein A-affinity chromatography and DEAE-cellulose chromatography. Purified, radiolabelled preparations of IgG were tested for binding to Gram-positive bacteria representing five different Fc-receptor (FcR) types. Distinct rat subclass-specific Fc-binding was noted to bacterial species belonging to different Fc-receptor types. Staphylococcus aureus (FcR I) strains bind IgGl and IgG2c as shown by others. Group C and G Streptococci (FcR III) bind all four subclasses of rat IgG. Streptococcus zooepidemicus strains (FcR V) also bind all four subclases but only to a lower degree. Human group A Streptococci (FcR II) and bovine... (More)
- The four IgG subclasses of the rat, IgGl, IgG2a, IgG2b and IgG2c, were purified from normal serum by a combination of protein A-affinity chromatography and DEAE-cellulose chromatography. Purified, radiolabelled preparations of IgG were tested for binding to Gram-positive bacteria representing five different Fc-receptor (FcR) types. Distinct rat subclass-specific Fc-binding was noted to bacterial species belonging to different Fc-receptor types. Staphylococcus aureus (FcR I) strains bind IgGl and IgG2c as shown by others. Group C and G Streptococci (FcR III) bind all four subclasses of rat IgG. Streptococcus zooepidemicus strains (FcR V) also bind all four subclases but only to a lower degree. Human group A Streptococci (FcR II) and bovine group G Streptococci (FcR IV) do not bind any of the rat IgG subclasses. Elution studies on two strains. Staphylococcus aureus, Cowan I, and human group G Streptococcus, G 148, showed that both thiocyanate and pH-elution might be useful for the fractionation of IgG subclasses bound to bacterial cells. The present work indicates the possible use of bacterial cells as solid-phase absorbents in immunological studies of rat IgG. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1102938
- author
- Nilsson, Rune LU ; Myhre, Erling LU ; Kronvall, Göran and Sjögren, Hans Olov LU
- organization
- publishing date
- 1982
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Immunology
- volume
- 19
- issue
- 1
- pages
- 119 - 126
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- pmid:7078553
- scopus:0020041354
- ISSN
- 1872-9142
- DOI
- 10.1016/0161-5890(82)90253-X
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Oncology, MV (013035000), Division of Infection Medicine (SUS) (013008000), Neurosurgery (013026000)
- id
- 2b637168-480b-419a-bcb5-15816c9985bf (old id 1102938)
- date added to LUP
- 2016-04-01 15:40:40
- date last changed
- 2021-01-03 06:09:14
@article{2b637168-480b-419a-bcb5-15816c9985bf, abstract = {{The four IgG subclasses of the rat, IgGl, IgG2a, IgG2b and IgG2c, were purified from normal serum by a combination of protein A-affinity chromatography and DEAE-cellulose chromatography. Purified, radiolabelled preparations of IgG were tested for binding to Gram-positive bacteria representing five different Fc-receptor (FcR) types. Distinct rat subclass-specific Fc-binding was noted to bacterial species belonging to different Fc-receptor types. Staphylococcus aureus (FcR I) strains bind IgGl and IgG2c as shown by others. Group C and G Streptococci (FcR III) bind all four subclasses of rat IgG. Streptococcus zooepidemicus strains (FcR V) also bind all four subclases but only to a lower degree. Human group A Streptococci (FcR II) and bovine group G Streptococci (FcR IV) do not bind any of the rat IgG subclasses. Elution studies on two strains. Staphylococcus aureus, Cowan I, and human group G Streptococcus, G 148, showed that both thiocyanate and pH-elution might be useful for the fractionation of IgG subclasses bound to bacterial cells. The present work indicates the possible use of bacterial cells as solid-phase absorbents in immunological studies of rat IgG.}}, author = {{Nilsson, Rune and Myhre, Erling and Kronvall, Göran and Sjögren, Hans Olov}}, issn = {{1872-9142}}, language = {{eng}}, number = {{1}}, pages = {{119--126}}, publisher = {{Pergamon Press Ltd.}}, series = {{Molecular Immunology}}, title = {{Fractionation of rat IgG subclasses and screening for IgG Fc-binding to bacteria}}, url = {{http://dx.doi.org/10.1016/0161-5890(82)90253-X}}, doi = {{10.1016/0161-5890(82)90253-X}}, volume = {{19}}, year = {{1982}}, }