Enzymic dephosphorylation of pepsin and pepsinogen.
It has been shown by the work presented in this paper that it is possible to dephosphorylate enzymically pepsin and pepsinogen with a variety of phosphatases. With the aid of a phosphodiesterase and the prostate phosphatase it has been established that the phosphorus in the two proteins is present as a diester and connects two sites of the peptide chain in a cyclic configuration. Removal of the phosphorus does not affect the proteolytic activity against hemoglobin or the synthetic substrate acetyl-L-phenylalanyl diiodotryosine, nor the pepsinogen pepsin transformation. However, an increase of the autodigestion of pepsin is observed.
D004792:Enzyme Precursors; D008297:Male; D010434:Pepsin A; D020116:Pepsinogen A; D010435:Pepsinogens; D010744:Phosphoric Monoester Hydrolases / Q000494:pharmacology*
D004792:Enzyme Precursors; D010435:Pepsinogens; D020116:Pepsinogen A; D010744:Phosphoric Monoester Hydrolases; D010434:Pepsin A
ENZYME PRECURSORS; PEPSINS; PHOSPHATASES/effects