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Monoclonal Antibody CFC - 6 , which Binds to Helix Ⅱ , Inhibits Erythropoietin - Induced Bioactivity
Kim, Suk Joon,Yoo, Ook Joon,Ha, Byung Jhip,Oh, Myung Suk,Kim, Hyun Su,Yoo, Ree Ann,Lee, Dong Eok,Park, Ji Sook,Woo, Koo 생화학분자생물학회 1998 BMB Reports Vol.30 No.5
It was discovered that monoclonal anti -erythropoietin (EPO) antibody CFC-6 can neutralize EPO-induced cell activation. To know the binding site of CFC-6, recombinant human erythropoietin (rhEPO) was digested with Glu-C. followed by a separation using high performance liquid chromato graphy (HPLC). Each HPLC fraction was blotted on the nitrocellulose membrane and the membrane was treated with anti-EPO antibody CFC-6 and anti-mouse antibody which is modified with peroxidase. Only one spot showed the color and the fraction was sequenced by Edman degradation. The results suggest that CFC-6 recognizes amino acid sequence V63-W-Q-G-L-A-L-L-S-E72 which is a part of helix II of the EPO molecule. Binding of CFC-6 to EPO may inhibit EPO binding to its receptor. which implies that the antibody binding site and the receptor binding site are close or overlapping.
Monoclonal Antibody CFC-6, which Binds to Helix II, Inhibits Erythropoietin-Induced Bioactivity
Ha, Byung-Jhip,Kim, Suk-Joon,Park, Ji-Sook,Yoo, Ree-Ann,Lee, Dong-Eok,Yoo, Ook-Joon,Woo, Koo,Kim, Hyun-Su,Oh, Myung-Suk Korean Society for Biochemistry and Molecular Biol 1997 Journal of biochemistry and molecular biology Vol.30 No.5
It was discovered that monoclonal anti-erythropoietin (EPO) antibody CFC-6 can neutralize EPO-induced cell activation. To know the binding site of CFC-6, recombinant human erythropoietin (rhEPO) was digested with Glu-C, followed by a separation using high performance liquid chromato graphy (HPLC). Each HPLC fraction was blotted on the nitrocellulose membrane and the membrane was treated with anti-EPO antibody CFC-6 and anti-mouse antibody which is modified with peroxidase. Only one spot showed the color and the fraction was sequenced by Edman degradation. The results suggest that CFC-6 recognizes amino acid sequence V63-W-Q-G-L-A-L-L-S-E72 which is a part of helix II of the EPO molecule. Binding of CFC-6 to EPO may inhibit EPO binding to its receptor, which implies that the antibody binding site and the receptor binding site are close or overlapping.
Lee, Dong-Eok,Ha, Byung-Jhip,Kim, Suk-Joon,Park, Ji-Sook,Yoo, Ree-Ann,Oh, Myung-Suk,Kim, Hyun-Su Korean Society for Biochemistry and Molecular Biol 1996 Journal of biochemistry and molecular biology Vol.29 No.3
A recombinant human erythropoietin (EPO), expressed in Chinese hamster ovary (CHO) cells, is glycosylated at Asn 24, Asn 38, Asn 83, and Ser 126. After release of the N-linked carbohydrate chains by $peptide-N^{4}-(N-acetyl-{\beta}-glucosaminyl)$ asparagine amidase F, the oligosaccharides were analyzed by FACE (Fluorophore-Assisted Carbohydrate Electrophoresis). The O-linked carbohydrate chain was separated by hydrazine, and analyzed by FACE. The monosacccharide composition of recombinant EPO showed man nose, fucose, galactose, N-acetylglucosamine, N-acetylneuraminic acid, and a trace of N-acetylgalactosamine, which are typical monosaccharides in the glycoproteins from the CHO cell. Sequences of N-linked and O-linked oligosaccharides were determined. The structure and composition of oligosaccharides attached to recombinant human EPO, expressed in the CHO cell, are identical to the reported oligosaccharide structure in human EPO isolated from urine.
Monoclonal Antibody CFC-6, which Binds to Helix II, Inhibits Erythropoietin-Induced Bioactivity
Oh,Myung-Suk,Park,Ji-Sook,Ha,Byung-Jhip,Yoo,Ook-Joon,Yoo,Ree-Ann,Lee,Dong-Eok,Kim,Suk-Joon,Woo,Koo,Kim,Hyun-Su The Korea Science and Technology Center 1997 BMB Reports Vol.30 No.5
It was discovered that monoclonal anti-erythropoietin (EPO) antibody CFC-6 can neutralize EPO-induced cell activation. To know the binding site of CFC-6, recombinant human erythropoietin (rhEPO) was digested with Glu-C, followed by a separation using high performance liquid chromato graphy (HPLC). Each HPLC fraction was blotted on the nitrocellulose membrane and the membrane was treated with anti-EPO antibody CFC-6 and anti-mouse antibody which is modified with peroxidase. Only one spot showed the color and the fraction was sequenced by Edman degradation. The result suggest that CFC-6 recognizes amino acid sequence V63-W-Q-G-L-A-L-L-S-E72 which is a part of helix Ⅱ of the EPO molecule. Binding of CFC-6 to EPO may inhibit EPO binding to its receptor, which implies that the antibody binding site and the receptor binding site are close or overlapping.
Kim, Suk Joon,Ha, Byung Jhip,Oh, Myung Suk,Kim, Hyun Su,Yoo, Ree Ann,Lee, Dong Eok,Park, Ji Sook 생화학분자생물학회 1981 BMB Reports Vol.29 No.3
A recombinant human erythropoietin (EPO), expressed in Chinese hamster ovary (CHO) cells, is glycosylated at Asn 24, Asn 38, Asn 83, and Ser 126. After release of the N-linked carbohydrate chains by peptide-N⁴-(N-acetyl-β-glucosaminyl) asparagine amidase F, the oligosaccharides were analyzed by FACE (Fluorophore-Assisted Carbohydrate Electrophoresis). The O-linked carbohydrate chain was separated by hydmzine, and analyzed by FACE. The monosacccharide composition of recombinant EPO showed mannose, fucose, galactose, N-acetylglucosamine, N-acetylneuraminic acid, and a trace of N-acetylgalactosamine, which are typical monosaccharides in the glycoproteins from the CHO cell. Sequences of N-linked and O-linked oligosaccharides were determined. The structure and composition of oligosaccharides attached to recombinant human EPO, expressed in the CHO cell, are identical to the reported oligosaccharide structure in human EPO isolated from urine.