Abstract
New relations for catalytic-activity analysis are proposed for simple association/dissociation equilibria between the mono- and oligo-meric forms of enzymes in the case where these equilibria evolve very slowly in comparison with the binding of the substrates. This analysis of activity versus total enzyme concentration leads rapidly to information, complementary to that given by physico-chemical methods, on specific activities, the degree of polymerization of the enzyme forms and on their dissociation constants.