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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
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Immunology
volume
19
issue
1
pages
119 - 126
publisher
Pergamon
external identifiers
  • pmid:7078553
  • scopus:0020041354
ISSN
1872-9142
DOI
10.1016/0161-5890(82)90253-X
language
English
LU publication?
yes
id
2b637168-480b-419a-bcb5-15816c9985bf (old id 1102938)
date added to LUP
2008-08-13 13:55:23
date last changed
2017-08-06 04:25:41
@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},
  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},
  volume       = {19},
  year         = {1982},
}