Activation of porcine pepsinogen A

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Abstract
Reaction products formed during activation of porcine pepsinogen A at pH 2 were characterized by native agar-gel electrophoresis and by denaturing SDS/PAGE. The results revealed the presence of non-covalent intermediates between prosegment peptides and pepsin. The complexes Leu1p-Leu44p/pepsin and Leu1p-Leu16p/pepsin were isolated (the prosegment residues are characterized by the suffix p; numbering of residues starts again from the N-terminus of pepsin). Relative to mature pepsin, the inherent milk-clotting activities of the intermediates were 3% and 18%, respectively. The intermediates were incubated at pH 8.5 for 20 min at 28 degrees C and the residual proteolytic activities were tested at pH 2. The stabilities at pH 8.5 were between those of pepsinogen and pepsin, Leu1p-Leu44p/pepsin being most stable. The implications of these findings for the conformational changes that occur during the activation of pepsinogen are discussed.