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Isolation and some properties of an IgG Fc-binding protein from group A streptococci type 15

Grubb, A LU orcid ; Grubb, R ; Christensen, P and Schalén, C LU orcid (1982) In International Archives of Allergy and Applied Immunology 67(4). p.76-369
Abstract

An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well... (More)

An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well as polyclonal IgG, IgG Fc and normal human serum. It did not precipitate IgG Fab, IgA, IgM, IgD or free kappa or lambda chains.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amino Acids, Antigens, Bacterial, Bacterial Outer Membrane Proteins, Bacterial Proteins/immunology, Binding Sites, Antibody, Carrier Proteins, Chemical Phenomena, Chemical Precipitation, Chemistry, Physical, Chromatography, DEAE-Cellulose, Electrophoresis, Polyacrylamide Gel, Humans, Immunodiffusion, Molecular Weight, Receptors, Fc, Receptors, IgG, Receptors, Immunologic, Streptococcus pyogenes/metabolism
in
International Archives of Allergy and Applied Immunology
volume
67
issue
4
pages
76 - 369
publisher
Karger
external identifiers
  • pmid:6461610
  • scopus:0020064599
ISSN
0020-5915
DOI
10.1159/000233049
language
English
LU publication?
yes
id
5de8c39c-75b3-409b-863a-848f841fab28
date added to LUP
2021-10-21 16:30:39
date last changed
2024-01-12 02:58:52
@article{5de8c39c-75b3-409b-863a-848f841fab28,
  abstract     = {{<p>An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well as polyclonal IgG, IgG Fc and normal human serum. It did not precipitate IgG Fab, IgA, IgM, IgD or free kappa or lambda chains.</p>}},
  author       = {{Grubb, A and Grubb, R and Christensen, P and Schalén, C}},
  issn         = {{0020-5915}},
  keywords     = {{Amino Acids; Antigens, Bacterial; Bacterial Outer Membrane Proteins; Bacterial Proteins/immunology; Binding Sites, Antibody; Carrier Proteins; Chemical Phenomena; Chemical Precipitation; Chemistry, Physical; Chromatography, DEAE-Cellulose; Electrophoresis, Polyacrylamide Gel; Humans; Immunodiffusion; Molecular Weight; Receptors, Fc; Receptors, IgG; Receptors, Immunologic; Streptococcus pyogenes/metabolism}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{76--369}},
  publisher    = {{Karger}},
  series       = {{International Archives of Allergy and Applied Immunology}},
  title        = {{Isolation and some properties of an IgG Fc-binding protein from group A streptococci type 15}},
  url          = {{http://dx.doi.org/10.1159/000233049}},
  doi          = {{10.1159/000233049}},
  volume       = {{67}},
  year         = {{1982}},
}