Selective removal of anti-α-Gal antibodies from human serum by using synthetic α-Gal epitope on a core-shell type resin
A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, α- and β-g...
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Published in | Biotechnology and bioprocess engineering Vol. 13; no. 4; pp. 445 - 452 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Heidelberg
The Korean Society for Biotechnology and Bioengineering
01.08.2008
한국생물공학회 |
Subjects | |
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Abstract | A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, α- and β-galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant α-(1,3)- and β-(1,4)-galactosyltransferases from E. coli. Finally, the synthesized α-Gal derivatives were immobilized on HiCore, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the α-Gal HiCore resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-I was used as the model binding protein. Furthermore, the α-Gal HiCore resin was more efficient at eliminating anti-α-Gal IgGs from the total human IgGs through immunoadsorption than the other two α-Gal resins, α-Gal TentaGel and α-Gal agarose. The α-Gal HiCore resin developed in this study can be utilized in a wide range of applications including ex vivo immunoadsorption and as a quantitative assay of anti-Gal antibody in human sera. |
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AbstractList | A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and
N
-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, α-and β-galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant α-(1,3)-and β-(1,4)-galactosyltransferases from
E. coli.
Finally, the synthesized α-Gal derivatives were immobilized on
Hi
Core, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the α-Gal
Hi
Core resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-I was used as the model binding protein. Furthermore, the α-Gal
Hi
Core resin was more efficient at eliminating anti-α-Gal IgGs from the total human IgGs through immunoadsorption than the other two α-Gal resins, α-Gal TentaGel and α-Gal agarose. The α-Gal
Hi
Core resin developed in this study can be utilized in a wide range of applications including
ex vivo
immunoadsorption and as a quantitative assay of anti-Gal antibody in human sera. A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, α- and β-galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant α-(1,3)- and β-(1,4)-galactosyltransferases from E. coli. Finally, the synthesized α-Gal derivatives were immobilized on HiCore, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the α-Gal HiCore resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-I was used as the model binding protein. Furthermore, the α-Gal HiCore resin was more efficient at eliminating anti-α-Gal IgGs from the total human IgGs through immunoadsorption than the other two α-Gal resins, α-Gal TentaGel and α-Gal agarose. The α-Gal HiCore resin developed in this study can be utilized in a wide range of applications including ex vivo immunoadsorption and as a quantitative assay of anti-Gal anti-body in human sera. KCI Citation Count: 6 A novel alpha -Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti- alpha -Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, alpha -and beta -galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant alpha -(1,3)-and beta -(1,4)-galactosyltransferases from E. coli. Finally, the synthesized alpha -Gal derivatives were immobilized on HiCore, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the alpha -Gal HiCore resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-I was used as the model binding protein. Furthermore, the alpha -Gal HiCore resin was more efficient at eliminating anti- alpha -Gal IgGs from the total human IgGs through immunoadsorption than the other two alpha -Gal resins, alpha -Gal TentaGel and alpha -Gal agarose. The alpha -Gal HiCore resin developed in this study can be utilized in a wide range of applications including ex vivo immunoadsorption and as a quantitative assay of anti-Gal antibody in human sera. A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, α- and β-galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant α-(1,3)- and β-(1,4)-galactosyltransferases from E. coli. Finally, the synthesized α-Gal derivatives were immobilized on HiCore, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the α-Gal HiCore resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-I was used as the model binding protein. Furthermore, the α-Gal HiCore resin was more efficient at eliminating anti-α-Gal IgGs from the total human IgGs through immunoadsorption than the other two α-Gal resins, α-Gal TentaGel and α-Gal agarose. The α-Gal HiCore resin developed in this study can be utilized in a wide range of applications including ex vivo immunoadsorption and as a quantitative assay of anti-Gal antibody in human sera. |
Author | Jang, K.S. (Seoul National University, Seoul, Republic of Korea) Chung, W.J. (Seoul National University, Seoul, Republic of Korea) Lee, Y.S. (Seoul National University, Seoul, Republic of Korea) Kim, Y.G. (Seoul National University, Seoul, Republic of Korea) Kim, H.K. (Seoul National University, Seoul, Republic of Korea) Kim, B.G. (Seoul National University, Seoul, Republic of Korea), E-mail: byungkim@snu.ac.kr |
Author_xml | – sequence: 1 fullname: Jang, K.S. (Seoul National University, Seoul, Republic of Korea) – sequence: 2 fullname: Chung, W.J. (Seoul National University, Seoul, Republic of Korea) – sequence: 3 fullname: Kim, H.K. (Seoul National University, Seoul, Republic of Korea) – sequence: 4 fullname: Kim, Y.G. (Seoul National University, Seoul, Republic of Korea) – sequence: 5 fullname: Lee, Y.S. (Seoul National University, Seoul, Republic of Korea) – sequence: 6 fullname: Kim, B.G. (Seoul National University, Seoul, Republic of Korea), E-mail: byungkim@snu.ac.kr |
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Snippet | A novel α-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-α-Gal antibodies in human serum for xenotransplantation. To... A novel alpha -Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti- alpha -Gal antibodies in human serum for... |
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SubjectTerms | alpha-Gal epitope anti-alpha-Gal antibody Biotechnology Chemistry Chemistry and Materials Science core-shell type resin Escherichia coli HiCore hyperacute rejection immunoadsorption Industrial and Production Engineering PROTEINAS PROTEINE PROTEINS xenotransplantation 생물공학 |
Title | Selective removal of anti-α-Gal antibodies from human serum by using synthetic α-Gal epitope on a core-shell type resin |
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