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Definition of IgG- and albumin-binding regions of streptococcal protein G

Åkerström, B LU ; Nielsen, E and Björck, L LU (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.

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author
; and
organization
publishing date
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
2024-01-01 06:53:20
@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}},
}