Definition of IgG- and albumin-binding regions of streptococcal protein G
(1987) In Journal of Biological Chemistry 262(28). p.91-13388- Abstract
Protein G, the immunoglobin G-binding surface protein of group C and G streptococci, also binds serum albumin. The albumin-binding site on protein G is distinct from the immunoglobulin G-binding site. By mild acid hydrolysis of the papain-liberated protein G fragment (35 kDa), a 28-kDa fragment was produced which retained full immunoglobulin G-binding activity (determined by Scatchard plotting) but had lost all albumin-binding capacity. A protein G (65 kDa), isolated after cloning and expression of the protein G gene in Escherichia coli, had comparable affinity to immunoglobulin G (5-10 X 10(10)M-1), but much higher affinity to albumin than the 35- and 28-kDa protein G fragments (31, 2.6, and 0 X 10(9)M-1, respectively). The... (More)
Protein G, the immunoglobin G-binding surface protein of group C and G streptococci, also binds serum albumin. The albumin-binding site on protein G is distinct from the immunoglobulin G-binding site. By mild acid hydrolysis of the papain-liberated protein G fragment (35 kDa), a 28-kDa fragment was produced which retained full immunoglobulin G-binding activity (determined by Scatchard plotting) but had lost all albumin-binding capacity. A protein G (65 kDa), isolated after cloning and expression of the protein G gene in Escherichia coli, had comparable affinity to immunoglobulin G (5-10 X 10(10)M-1), but much higher affinity to albumin than the 35- and 28-kDa protein G fragments (31, 2.6, and 0 X 10(9)M-1, respectively). The amino-terminal amino acid sequences of the 65-, 35-, and 28-kDa fragments allowed us to exactly locate the three fragments in an overall sequence map of protein G, based on the partial gene sequences published by Guss et al. (Guss, B., Eliasson, M., Olsson, A., Uhlen, M., Frej, A.-K., Jörnvall, H., Flock, J.-I., and Lindberg, M. (1986) EMBO J. 5, 1567-1575) and Fahnestock et al. (Fahnestock, S. R., Alexander, P., Nagle, J., and Filpula, D. (1986) J. Bacteriol. 167, 870-880). In this map could then be deduced the location of three homologous albumin-binding regions and three homologous immunoglobulin G-binding regions.
(Less)
- author
- Åkerström, B LU ; Nielsen, E and Björck, L LU
- organization
- publishing date
- 1987-10-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Amino Acid Sequence, Antigens, Bacterial, Bacterial Proteins/immunology, Binding Sites, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Humans, Immunoglobulin G/metabolism, Kinetics, Molecular Weight, Serum Albumin/metabolism
- in
- Journal of Biological Chemistry
- volume
- 262
- issue
- 28
- pages
- 91 - 13388
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:0023645661
- pmid:3654618
- ISSN
- 0021-9258
- language
- English
- LU publication?
- yes
- id
- f532b9e7-5fc4-4bb0-85a4-4e6ca9dcc5ca
- alternative location
- http://www.jbc.org/content/262/28/13388.long
- date added to LUP
- 2019-05-22 10:31:01
- date last changed
- 2024-09-18 21:44:57
@article{f532b9e7-5fc4-4bb0-85a4-4e6ca9dcc5ca, abstract = {{<p>Protein G, the immunoglobin G-binding surface protein of group C and G streptococci, also binds serum albumin. The albumin-binding site on protein G is distinct from the immunoglobulin G-binding site. By mild acid hydrolysis of the papain-liberated protein G fragment (35 kDa), a 28-kDa fragment was produced which retained full immunoglobulin G-binding activity (determined by Scatchard plotting) but had lost all albumin-binding capacity. A protein G (65 kDa), isolated after cloning and expression of the protein G gene in Escherichia coli, had comparable affinity to immunoglobulin G (5-10 X 10(10)M-1), but much higher affinity to albumin than the 35- and 28-kDa protein G fragments (31, 2.6, and 0 X 10(9)M-1, respectively). The amino-terminal amino acid sequences of the 65-, 35-, and 28-kDa fragments allowed us to exactly locate the three fragments in an overall sequence map of protein G, based on the partial gene sequences published by Guss et al. (Guss, B., Eliasson, M., Olsson, A., Uhlen, M., Frej, A.-K., Jörnvall, H., Flock, J.-I., and Lindberg, M. (1986) EMBO J. 5, 1567-1575) and Fahnestock et al. (Fahnestock, S. R., Alexander, P., Nagle, J., and Filpula, D. (1986) J. Bacteriol. 167, 870-880). In this map could then be deduced the location of three homologous albumin-binding regions and three homologous immunoglobulin G-binding regions.</p>}}, author = {{Åkerström, B and Nielsen, E and Björck, L}}, issn = {{0021-9258}}, keywords = {{Amino Acid Sequence; Antigens, Bacterial; Bacterial Proteins/immunology; Binding Sites; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Humans; Immunoglobulin G/metabolism; Kinetics; Molecular Weight; Serum Albumin/metabolism}}, language = {{eng}}, month = {{10}}, number = {{28}}, pages = {{91--13388}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Definition of IgG- and albumin-binding regions of streptococcal protein G}}, url = {{http://www.jbc.org/content/262/28/13388.long}}, volume = {{262}}, year = {{1987}}, }