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A 32-kDa protein was isolated from human monocytes after calcium precipitation and chromatography. The protein activity was assessed by the inhibition of soluble phospholipase A 2 (PLA2). This in vitro inhibitory effect on phospholipases A 2 was found only with negatively charged phospholipids. The protein was also able to inhibit cellular PLA~ in mouse thymocytes. The biochemical properties and amino acid composition strongly suggest that the protein shares similarities with endonexin. Using a neutralizing monoclonal antibody against rat lipocortin, we found a cross-reactivity with the 32-kDa protein. According to the biochemical and immunological properties, we propose to relate this PLA 2 inhibitory protein from human monocytes to lipocortin.