Purification of Murine MHC Antigens by Monoclonal Antibody Affinity Chromatography

Matthew F. Mescher, Kathryn C. Stallcup, Cathleen P. Sullivan, Aaron P. Turkewitz, Steven H. Herrmann

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


This chapter discusses the purification of murine major histocompatibility complex (MHC) antigens by monoclonal antibody affinity chromatography. The growing understanding of the role of MHC antigens in transplantation and immune system recognition has resulted in considerable interest in the functional and structural characteristics of these cell-surface glycoproteins. Monoclonal antibody affinity chromatography has proved to be a rapid and efficient means of purifying relatively large amounts of both class I and class II murine MHC antigens. There is a successfully use of four monoclonal antibodies as affinity reagents. The same general approach is applicable to the purification of a variety of MHC antigens using different monoclonal antibodies. The antigens purified in this way retain serological and biological activity and prove to be useful for studying the structure and function of these molecules.

Original languageEnglish (US)
Pages (from-to)86-109
Number of pages24
JournalMethods in enzymology
Issue numberC
StatePublished - Jan 1 1983


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