<p>Pancreatitis-associated protein (PAP) is a lectin-related secretory proteinpresent in small amounts in normal pancreas and overexpressed during the acute phase of the pancreatitis [<cite idref="PUB00007643"/>, <cite idref="PUB00007644"/>]. Conversely, PAP is constitutively expressed in the intestinal tract, but not in other tissues [<cite idref="PUB00007644"/>]. PAP mRNA could not be evidenced in liver, stomach, salivary glands, brain, kidney or testis. Its pattern of expression during severe pancreatic aggression suggests that it might be a stress protein involved in the control of bacterial proliferation [<cite idref="PUB00007645"/>].</p><p>The deduced amino acid sequence of PAP shows marked similarity to thecarbohydrate-recognition domain (CRD) of animal lectins [<cite idref="PUB00007645"/>]. Animal lectins display a wide variety of architectures, and are classified according to the CRD, of which there are two principal types: S-type and C-type. C-type lectins require Ca2+ for their activity. The CRD consists of 110-130 residues, which include four perfectly conserved cysteines that are involved in the formation of two disulphide bridges. </p>