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Development of a two‐step chromatography procedure that allows the purification of a high‐purity anti‐histone H1 monoclonal immunoglobulin M antibody with immunosuppressant activity
Author(s) -
Shimada Yayoi,
Goto Takeshi,
Kawamoto Seiji,
Kiso Takashi,
Katayama Akiko,
Yamanaka Yasushi,
Aki Tsunehiro,
Chiang KueiChen,
Nakano Toshiaki,
Goto Shigeru,
Chen ChaoLong,
Ohmori Naoya,
Ono Kazuhisa,
Sato Shuji
Publication year - 2008
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.887
Subject(s) - monoclonal antibody , polyclonal antibodies , chemistry , antibody , affinity chromatography , monoclonal , transplantation , isotype , chromatography , microbiology and biotechnology , biochemistry , immunology , biology , medicine , surgery , enzyme
In organ transplantation, the development of a novel immunosuppressant free of the need for permanent administration and any serious side effects has eagerly been awaited. We have previously reported that an anti‐histone H1 polyclonal antibody has immunosuppressant activity. Here we prepared an anti‐histone H1 monoclonal antibody as an analytical tool to elucidate its mechanism of immunosuppression. The isotype of this monoclonal antibody was immunoglobulin M. A monoclonal antibody prepared for administration to organ transplantation model animals should not contain any allogenic proteins and should have high purity. Therefore, we conducted a two‐step chromatography procedure, consisting of strong anion‐exchange chromatography and gel filtration chromatography, to purify an anti‐histone H1 monoclonal immunoglobulin M antibody from the serum‐free culture supernatant of hybridomas. Consequently, we successfully purified the monoclonal antibody at 96%, a purification rate at which its administration to organ transplantation model animals is possible. Copyright © 2007 John Wiley & Sons, Ltd.