Abstract
mRNA from pig duodenal mucosa directs synthesis, in a wheat-germ cell-free system, of two products precipitated by antiserum to pure calcium-binding protein. One of these products has a higher molecular weight than authentic calcium-binding protein, but, like the authentic protein, is heat-stable. The other protein co-migrates with pure calcium-binding protein on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, is stable on heating to 70 degrees C for 15 min and alters its elution position on ion-exchange chromatography depending on whether Ca2+ is present in or absent from the elution buffer. The synthesized protein has these properties in common with authentic calcium-binding protein.