Ito H, Ooyama T, Orimo H
Endocrinol Jpn. 1976 Apr;23(2):109-14. doi: 10.1507/endocrj1954.23.109.
Biological activity of porcine calcitonin was most actively inactivated by the rat kidney homogenate than by other tissue homogenates. Among the various subcellular fractions of the rat kidney homogenate examined, microsome fraction was most active in the in vitro inactivation of porcine calcitonin. Inactivation of porcine calcitonin by the rat kidney microsome was dependent on pH and temperature. Inactivating activity of the rat kidney microsome was inhibited by 1 X 10(-3) M monoiodoacetate and 1 X10(-5) M p-chloromercuribenzoate. These results suggest that porcine calcitonin is probably inactivated by a SH-enzyme in the rat kidney microsomes. However, the participation of other enzymes cannot be ruled out, since the inactivating activity of the rat kidney microsome fraction is also inhibited by 1 X 10(-4) M diisopropylfuorophosphate.
猪降钙素的生物活性在大鼠肾脏匀浆中比在其他组织匀浆中更易被快速灭活。在所检测的大鼠肾脏匀浆的各种亚细胞组分中，微粒体组分在体外对猪降钙素的灭活作用最为活跃。大鼠肾脏微粒体对猪降钙素的灭活作用取决于pH值和温度。大鼠肾脏微粒体的灭活活性受到1×10⁻³ M碘乙酸盐和1×10⁻⁵ M对氯汞苯甲酸的抑制。这些结果表明，猪降钙素可能被大鼠肾脏微粒体中的一种巯基酶灭活。然而，由于大鼠肾脏微粒体组分的灭活活性也受到1×10⁻⁴ M二异丙基氟磷酸的抑制，所以不能排除其他酶的参与。
