During the course of gestation, changes in the metabolism and chemical composition of the cervical connective tissue occur. The concentrations of collagen, proteoglycan and hyaluronate in the cervix decrease with time of pregnancy, while there is a small but significant increase in tissue hydration. The collagen network loses its dense, ordered appearance and assumes a loose, frayed, disoriented structure. A small molecular weight dermatan sulphate proteoglycan with Kav = 0.48 on Sepharose CL-4B has been isolated from pregnant and nonpregnant ovine cervix. Proteoglycans isolated from dilated cervix yield a second peak at the excluded volume of a Sepharose CL-4B column which may represent a new proteoglycan species, or represent a proteoglycan monomer with larger glycosaminoglycan constituents. The rate of synthesis of proteoglycan is enhanced during pregnancy, and doubles in the time between 140 days and term (dilated). The increased rate of proteoglycan synthesis in the presence of a diminishing hexuronate concentration in the pregnant cervix is indicative of enhanced proteoglycan turnover. This may provide some insight into the mechanism whereby a new matrix with altered mechanical properties is produced, since a rapid turnover of matrix components enables a remodeling of the connective tissue framework. This reorganization of the matrix is discussed with respect to parturition.