During development of the pregnant rat uterus there is a several fold increase in elastin content. Using Verhoeff's elastic fiber stain, we have shown that a significant proportion of these elastin fibers are in the extracellular matrix of the myometrium. They do not appear as an organized structure but rather in a variety of partially extended, random configurations. An elastase was identified in both the pregnant and the postpartum uterus. Partial characterization of the enzyme indicated that it is a serine protease with a molecular weight around 24,500 and a pH optimum of 8.5. In addition to the enzyme, relatively high levels on an elastase inhibitor were found in the uterine extracts. The inhibitor did not inhibit trypsin, indicating that it was not alpha-1-antiprotease. The data suggest that the elastase and inhibitor are uterine tissue derived and perhaps important in the normal remodeling process of uterine connective tissue.