Abstract
There are conflicting reports concerning the number of distinct Δ 53-oxosteroid isomerases present in various steroid producing tissues; this problem was reexamined by two techniques: (1) kinetic measurements with a mixture of androst-5-ene-3,17-dione and pregn-5-ene-3,20-dione. (2) thermal inactivation of the androst-5-ene-3, 17-dione isomerase and pregn-5-ene-3, 20-dione isomerase activities. The results are the following: (a) Kinetic data support the concept of a single Δ 53-oxosteroid isomerase with a low substrate specificity in the microsomes. (b) Thermal inactivation experiments also support the one enzyme theory, but strongly suggest an heterogeneity of the Δ 53-oxosteroid isomerase in the bovine adrenocortical microsomes. In view of these results, a tentative explanation of the conflicting reports is proposed.
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