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Serveral different types of collagen have been identified invivo. Human    placenta has been employed by a number of investigators over the past    decade as a starting material for isolation and characterization of different    genetic types of collagen including type I,III,IV and IV molecules.           Proteases of the placenta participate in the degradation of intracellular    and extracelluar matrix proteins. To extract collagen types IV and I+III , a    healthy placenta at term (38 weeks) and a premature placenta (14 weeks)    were placed under pepsin digestion using minimum quantity. The steps of    extraction were controlled by the SDS-PAGE.           The electrophoretical patterns of premature placental collagen    indicated that the number of collagen chains types IV and I+III in premature    placenta were less than that of the healthy placenta at term.  According    to electrophoretical pattern in the premature placenta , there were not    a2(IV) , b11(I) , b12(I) and a1(III) chains. Thus , it is probable that in some of the    repeating abortion the synthesis of collagen is decreased or degradation of    collagen is increased.           So it is suggested to measure the serum and cervix collagenase in    women who had unexplained abortions.