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Fractionation of rat IgG subclasses and screening for IgG Fc-binding to bacteria

Nilsson, Rune LU ; Myhre, Erling LU ; Kronvall, Göran and Sjögren, Hans Olov LU (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)
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author
; ; and
organization
publishing date
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}},
}