Abstract
SummaryNeutral proteolytic activity in the liver exists in an active and an inactive form which can be reactivated by the addition of ATP. The acute stress elicited by complete body restraint produced a significant decrease in the active form of the proteinases conceivably reducing the rate of protein catabolism at neutral pH. Full levels of proteolytic activity could be restored by the addition of exogenous ATP to the homogenates. The fact that stress situations produce a large release of steroids able to increase the rate of protein synthesis in the liver has suggested that the decreased proteolytic activity could be due to a decreased availability of the proteinase activator, at this point believe to be the aspartyl adenylate.
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