Expression of a fusion protein of scFv–biotin mimetic peptide for immunoassay

We constructed two fusion proteins of scFv linked to biotin mimetic sequence (BMS) via different linkers, and expressed them in the Pichia pastoris expression/secretion system. We found that both bi-functional scFv proteins exhibited their intrinsic binding activities to antigen CA125 determined in...

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Veröffentlicht in:	Journal of biotechnology 1998-10, Vol.65 (2), p.225-228
Hauptverfasser:	Luo, D, Geng, M, Schultes, B, Ma, J, Xu, D.Z, Hamza, N, Qi, W, Noujaim, A.A, Madiyalakan, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Bispecific - immunology Antigens Binding energy Bioassay Biological and medical sciences Biotechnology Biotin - chemistry Biotin - metabolism Biotin mimetic CA-125 Antigen - immunology Fundamental and applied biological sciences. Psychology Fusion protein Genetic technics applied to diagnosis Health. Pharmaceutical industry Humans Immunoglobulin Fragments - immunology Immunoglobulin Fragments - metabolism Immunoglobulin Variable Region - immunology Immunoglobulin Variable Region - metabolism Immunology Industrial applications and implications. Economical aspects Pichia - genetics Pichia - metabolism Pichia expression Proteins Proto-Oncogene Proteins c-myc Radioimmunoassay - methods Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - immunology Single chain Fv Streptavidin - metabolism
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Zusammenfassung:	We constructed two fusion proteins of scFv linked to biotin mimetic sequence (BMS) via different linkers, and expressed them in the Pichia pastoris expression/secretion system. We found that both bi-functional scFv proteins exhibited their intrinsic binding activities to antigen CA125 determined in competitive radioimmunoassay experiments, but the fusion protein with a spacer between the scFv and BMS (scFv–spacer–BMS) showed higher binding activity of streptavidin than the one with c-Myc peptide as a linker.
ISSN:	0168-1656 1873-4863
DOI:	10.1016/S0168-1656(98)00094-7