A bifunctional affinity linker to couple antibodies to cellulose.
We have constructed a fusion protein between the staphylococcal A protein and the cellulose binding domain of an exoglucanase (Cex) from Cellulomonas fimi that can be directly immobilized on cellulose while retaining its capacity to bind immunoglobulin G molecules. The cellulose domain provides binding that does not interfere with the biological activity of the fusion partner, does not involve hazardous chemicals and the matrix does not need to be chemically activated which reduces its cost. We have tested some of the possible applications of the fusion protein and show that it can be used in immunoassays, affinity chromatography and immunoprecipitations.
Ramírez
C
C
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Fung
J
J
Miller
R C
RC
Antony
R
R
Warren
J
J
Kilburn
D G
DG
D000906:Antibodies / Q000378:metabolism; D001665:Binding Sites; D002482:Cellulose / Q000378:metabolism; D002846:Chromatography, Affinity; D043326:Glucan 1,3-beta-Glucosidase; D007074:Immunoglobulin G / Q000378:metabolism; D007163:Immunosorbent Techniques; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000378:metabolism*; D013205:Staphylococcal Protein A / Q000235:genetics* / Q000378:metabolism; D001617:beta-Glucosidase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D000906:Antibodies; D007074:Immunoglobulin G; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D002482:Cellulose; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase