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Human plasma amyloid P component (APP) is a complement regulatory protein, which may also interact with matrix metalloproteinases (MMP) and lipase to inhibit their activity. To clarify which APP functions, we studied the (Ca2+ + Mg2+)-dependent hydrolytic and enzymatic activities of purified (Ca2+ + Mg2+)-dependent plasma (APP) and serum (APPS) amyloid P components. APP was isolated by affinity chromatography on 1D4 monoclonal antibody-conjugated Sepharose 4B. (Ca2+ + Mg2+)-dependent hydrolytic activities of purified APP and APPS by using native Gt-B gel electrophoresis and zymography. Enzymatic activities were assayed using gelatin (gelatinolytic) and casein (caseinolytic) substrates. Purified APP bound 1D4 and inhibited the binding of labeled 1D4 to immobilized APP. In (Ca2+ + Mg2+)-dependent hydrolytic activity assays, APP hydrolyzed casein about 2-fold more effectively than gelatin. Purified APP hydrolyzed casein, gelatin and type I procollagen at comparable rates. Purified APPS also hydrolyzed both substrates. The inhibitory activities of APPS on both gelatin and casein were comparable with those of purified APP.