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Methods to quantitate human haptoglobin by complexation with hemoglobin.

作者信息

Cerda S, Oh S K

机构信息

Department of Microbiology, Boston University School of Medicine, MA 02118.

出版信息

J Immunol Methods. 1990 Nov 6;134(1):51-9. doi: 10.1016/0022-1759(90)90111-8.

DOI:10.1016/0022-1759(90)90111-8
PMID:2230149
Abstract

Native human haptoglobin isolated from normal human plasma by affinity chromatography on chicken hemoglobin -Sepharose was used as standard antigen. A direct sandwich ELISA for haptoglobin was developed, with human hemoglobin as a capturing agent. The peroxidase activity of the complex was measured as a means of detecting functional haptoglobin. The reactivities of monoclonal antibody vs. polyclonal antisera on the haptoglobin-hemoglobin complex were compared. Adopting a monoclonal antibody, clone 21.7, which is directed to the alpha chain of haptoglobin, a specific method to quantitate the native haptoglobin which can complex with hemoglobin has been developed.

摘要

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