The kinetic characteristics of substrate utilization by hepatic adenylate cyclase were investigated under a variety of incubation conditions, including variations in pH, [substrate], [Mg2+], and in the absence or presence of glucagon. Activities were compared with ATP and 5' adenylylimidodiphosphate [App(NH)p] as substrates. The K(m) for both substrates was about 50 μM; V(max) given with App(NH)p was about 40% lower than obtained with ATP as substrate.
|Number of pages||7|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 1975|
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