Apr 1, 1976

Inactivation of porcine calcitonin by rat kidney microsome

Endocrinologia Japonica
H ItoH Orimo


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.

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Mentioned in this Paper

Pork calcitonin
Enzymes, antithrombotic
Alkaline Phosphatase
Enzymes for Treatment of Wounds and Ulcers
Iodoacetic Acids
Subcellular Fractions

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