Inactivation of Porcine Calcitonin by Rat Kidney Microsome
スポンサーリンク
概要
- 論文の詳細を見る
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 <I>in vitro</I> 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 1×10<SUP>-3</SUP>M monoiodoacetate and 1×10<SUP>-5</SUP>M p-chloromercuribenzoate. These results suggest that porcine calcitonin is probably inactivated by a SH-enzyme in the rat kidney microsome. However, the participation of other enzymes cannot be ruled out, since the inactivating activity of the rat kidney microsome fraction is also inhibited by 1×10<SUP>-4</SUP>M diisopropylfluorophosphate.
- 社団法人 日本内分泌学会の論文
著者
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ORIMO HAJIME
Section of Endocrinology, Tokyo yoikin Hospital
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ITO HIDEKI
Section of Endocrinology, Tokyo Metropolitan Geriatric Hospital
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OOYAMA TOSHIRO
Section of Endocrinology, Tokyo Metropolitan Geriatric Hospital
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ORIMO HAJIME
Section of Endocrinology Tokyo Metropolitan Geriatric Hospital
関連論文
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- Calcitonin Inhibition of Gastrin Secretion in Man