RECOMBINANT C-TERMINAL DOMAIN OF PANCREATIC LIPASE RETAINS FULL ABILITY TO BIND COLIPASE

The organization of the pancreatic lipase in two well defined domains has been correlated to a specific function for each domain, catalytic activity for the N-terminal domain and colipase binding for the C-term inal domain, In order to see if such an organization implies that the two domains can behave as separate entities, we expressed the N- and C -terminal domains in insect cells. The recombinant proteins secreted i n the cell supernatants present the expected molecular properties. How ever, whereas the C-terminal domain retains its function of colipase b inding, the N-terminal domain appears to be unable to ensure catalysis , The lack of activity of the recombinant N-terminal domain could resu lt either from a (partially) incorrect folding or from an incapacity t o function by itself. These results suggest that, although both are st ructurally well defined, the two domains of the pancreatic lipase beha ve differently when they are expressed as separate entities.