| Abstract: | A CaCO3-crystal growth inhibitor has recently been isolated from the calculi of patients affected by pancreatic lithiasis. It is a phosphoglycoprotein, with a molecular weight of 14,000, whose probable physiological role is the stabilization of exocrine pancreatic secretion which is supersaturated with respect to CaCO3. In order to isolate this inhibitor from human pancreatic juice, monoclonal antibodies to the protein were prepared and an immunoadsorbent column was developed. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of proteins fixed by the immunoadsorbent reveals the form having a molecular weight of 14,000, in addition to other protein bands which have higher molecular weights (16,000, 16,800, 18,000, and 18,800). All of these different proteins are also recognized by a monospecific polyclonal antibody to the 14,000 molecular weight form. Using the same monospecific polyclonal antibody only one messenger RNA coding for this inhibitor has been demonstrated. Thus, this heterogeneity might be explained by post-translational modifications. |
