Insulin-like Activity of Proteases. V. Stimulation of Cyclic Adenosine 3', 5'-Monophosphate Phosphodiesterase by an N-Succinyl-L-alanyl-L-alanyl-L-alanine p-Nitroanilide-hydrolyzing Protease

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The stimulatory effect of an N-succinyl-L-alanyl-L-alanyl-L-alanine p-nitroanilidehydrolyzing protease (STA-protease), which was partially purified from Pronase, on cyclic adenosine 3', 5'-monophosphate (cyclic AMP) phosphodiesterase of bovine heart was investigated by measuring the changes in kinetic constants. The phosphodiesterase used showed hydrolytic activity towards cyclic AMP at a concentration of 1 or 100 μM. STA-protease stimulated low K_m phosphodiesterase but not high K_m phosphodiesterase activity, in the presence of ethylene glycol bis (β-aminoethylether)-N, N'-tetraacetic acid (EGTA). No stimulation of the low K_m enzyme was observed when theophylline was used instead of EGTA. Proteases such as Pronase, trypsin, chymotrypsin, elastase, and substilisin BPN' stimulated the low K_m enzyme to various extents. Although STA-protease showed the lowest caseinolytic activity among proteases tested, its stimulatory activity towards the low K_m enzyme was rather high. STA-protease increased the K_m and V_max values of the low K_m enzyme, whereas trypsin decreased the K_m value without causing significant change in V_max. The stimulatory mechanism of STA-protease probably differs from that of trypsin.
社団法人日本薬学会の論文
1982-03-25