Limunectin. A phosphocholine-binding protein from Limulus amebocytes with adhesion-promoting properties.

摘要: Abstract A protein that binds to and precipitates with pneumococcal C-polysaccharide a phosphocholine (PC) derivative of bovine serum albumin has been affinity purified from Limulus amebocytes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis reveals the isolated consists single polypeptide chain approximately 50 kDa. It is an intracellular localized in secretory granules amebocytes according immunogold staining. Although it shares PC-binding property C-reactive other animal species, differs latter PC only presence Ca2+, whereas newly Ca(2+)-independent manner. In this respect, resembles antibodies mouse myelomas. The gene coding for isolated. sequence predicts 54 kDa unusual structural feature: almost entirely 10 contiguous segments, 45 amino acids length, extensive homology. Some limited homologies were found between 54-kDa segments vitronectin, gelatinase, collagenase. bacterial cells, fixed amebocytes, number extracellular matrix molecules. Due its some functional similarities adhesion molecules, was named "Limunectin."