In a recent study of the effects of various ligands on the rate of proteolytic digestion of rabbit muscle aldolase, it was observed that dihydroxyacetone phosphate (DHAP) acts as a powerful inhibitor of bovine pancreatic carboxypeptidase A (CPA) (Adelman et al., 1968). The present work demonstrates that this inhibition is competitive for both peptidase and esterase activities. Because this represents the first observation of competitive inhibition of CPA by a compound lacking an aromatic group, it was of interest to characterize further the structural requirements for this interaction.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 25 Nov 1968|