Abstract
Total, active and latent collagenase activities were determined by direct assay of tissue homogenates. The rate of collagen breakdown during post-partum involution of the rat uterus is correlated with the total activity of collagenase. Both are low at parturition, reach a maximum within 24 h and fall slowly to low values by 5 days post partum. Collagenase apparently participates in collagen breakdown in vivo. Estradiol-17.beta. (100 .mu.g/day, i.p.), which inhibits the breakdown of collagen by 36% during the first 4 days of involution, produces a closely corresponding decrease in total collagenase activity. The effect of estradiol in lowering collagenase activity is not due to alterations in collagen substrate, collagenase kinetic behavior or latent-to-active enzyme conversion. Of the total assayable collagenase, about 35% is fully active and 65% is in a latent form. About 70% of this latent from can be activated by a serine proteinase found, together with collagenase, in the insoluble fraction of uterine homogenates.