Abstract
The various forms of proteinases in the chorioamniotic membranes (CAM) have been investigated utilizing specific and nonspecific substrates and group-specific inhibitors. We have demonstrated the presence of acid, serine, thiol, and metalloproteinases in CAM. It is indicated in fractionation studies that, in the CAM, most of the thiol and alkaline-proteolytic activity is of lysosomal origin, while the acid proteinases are of lysosomal and cytosolic origin. The alkaline-proteolytic activity appears to be associated with the fibroblasts. By the activity patterns and inhibition studies demonstrated by us, the presence in the CAM of almost all classes of proteinases is indicated; among these classes, thiol and metalloproteinases seem to be the major ones. We evaluated the possible involvement of these proteinases in the process leading to the rupture of CAM.
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