Abstract
Previously, aminopeptidase P (AmP) has been purified from mammalian tissues by highly laborious multistep chromatography procedures. To simplify purifications, we raised a monoclonal antibody to guinea pig serum AmP and used the antibody to prepare an immunoaffinity matrix. The immunoaffinity matrix was used to obtain highly purified forms of AmP from guinea pig lungs, kidney and serum. The antibody is reactive with rat and human forms of AmP and may simplify procedures needed for their purifications.
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