Isolation and some properties of an IgG Fc-binding protein from group A streptococci type 15
(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.
(Less)
- author
- Grubb, A LU ; Grubb, R ; Christensen, P and Schalén, C LU
- organization
- publishing date
- 1982
- 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
-
- scopus:0020064599
- pmid:6461610
- 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}}, }