|
|
The gene for the bacterial surface receptor streptococcal protein
G was cloned and characterized (1). The separate interactions
with human IgG and Human Serum Albumin (HSA) were analyzed and
determined (1,2,3). Engineered versions of the receptor was
developed (3) and chimeric receptors containing the IgG-binding
domains of both staphylococcal protein A and streptococcal protein
G were constructed (2). Recombinant protein G lacking the serum
albumin-binding domains was developed in collaboration with
Pharmacia Biotech (Uppsala, Sweden), now GE Health Care. Recombinant
protein G is now frequently used for affinity purification of
antibodies and antibody fragments.
| Key publications: |
| 1. |
Guss, B., M. Eliasson, A. Olsson,
M. Uhlen, A.K. Frej, H. Jornvall, J.I. Flock, and M. Lindberg
(1986) Structure of the IgG-binding regions of streptococcal
protein G. EMBO J 5, 1567-1575. |
| 2. |
Eliasson, M., R. Andersson, A. Olsson, H.
Wigzell, and M. Uhlen (1988) Chimeric IgG-binding receptors
engineered from staphylococcal protein A and streptococcal
protein G. J Biol Chem 263, 4323-4327. |
| 3. |
Eliasson, Andersson, Olsson, Wigzell &
Uhlen (1989) Differential IgG-binding characteristics of
staphylococcal protein A, streptococcal protein G, and a
chimeric protein AG. J Immunol 142, 575-581. |
|
