In recent years the cathepsin type proteases (intracellular acid proteases present in the animal tissues**) have been reported to exist in a variety of animal tissues, and some of these proteases have been highly purified1-3). Moreover, some reports on their distribution in the cell4,5) or on their enzymological properties1-3.6) have been accumulated. The presence of an acid protease activity (i.e., catheptic activity) has also been reported in the ovaries of human7,8), sows7,8), dairy cows9), and rats10,11), and the relationship between the activities of both the cathepsin type and the alkaline proteases and the ovarian function or the response to the gonadotropin treatment has been discussed. The properties of these enzymes in the ovary, however, have been little known yet, and the physiological significances of these enzymes are still a matter of speculation.From these points of view, we paid attention to the physiological relations between the ovarian function and the proteolytic enzymes of the ovary, and conducted the investigations on the proteolytic activities present in the ovary of the immature rats pretreated with gonadotropins by using the more sensitive assay method than the measurement of light absorption at 280nm and by using the assay medium without urea. During the course of these experiments, a catheptic activity was found in the supernatant fluid of the rat ovarian homogenate used in the experiment, but the alkaline protease activity was little detected in the fluid. The present report describes the level and some properties of the catheptic activity of the ovary.