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The gene for the staphylococcal protein A was cloned and characterized
(1, 2, 3, 4). This IgG-binding receptor was found to have evolved
through multiple gene duplications (2). Several recombinant
versions of the receptor (5) were developed in collaboration
with Pharmacia Biotech (Uppsala, Sweden), now GE Health Care.
Recombinant protein A (see figures) is now frequently used for
affinity purification of monoclonal and polyclonal antibodies.
| Key (own)
publications: |
| 1. |
Lofdahl, Guss, Uhlen, Philipson
& Lindberg (1983) Gene for staphylococcal protein A.
Proc Natl Acad Sci U S A 80, 697-701. |
| 2. |
Uhlen, M., B. Guss, B. Nilsson, S. Gatenbeck,
L. Philipson, and M. Lindberg (1984) Complete sequence of
the staphylococcal gene encoding protein A. A gene evolved
through multiple duplications. J Biol Chem 259, 1695-1702. |
| 3. |
Abrahmsen, Moks, Nilsson, Hellman & Uhlen
(1985) Analysis of signals for secretion in the staphylococcal
protein A gene. Embo J 4, 3901-3906. |
| 4. |
Moks, T., L. Abrahmsen, B. Nilsson, U. Hellman,
J. Sjoquist, and M. Uhlen (1986) Staphylococcal protein
A consists of five IgG-binding domains. Eur J Biochem 156,
637-643. |
5. |
Nilsson, B., T. Moks, B. Jansson, L. Abrahmsen,
A. Elmblad, E. Holmgren, C. Henrichson, T.A. Jones, and
M. Uhlen (1987) A synthetic IgG-binding domain based on
staphylococcal protein A. Protein Eng 1, 107-113. |
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