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      Loss of Immunoreactivity of Human Serum Parathyroid Hormone by the Action of Rat Kidney Enzyme, Preferentially Hydrolyzing Parathyroid Hormone

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          Acetone powder of rat kidney was extracted with0.15 m KCl containing 5 mM tris-Cl and 15% glycerol. The fraction, precipitated by 35-75% saturated ammonium sulfate, was chromatographed on a Biogel P-300 column to obtain a partially purified rat kidney enzyme preparation preferentially hydrolyzing parathyroid hormone. Parathyroid hormone in human serum lost its immunoreactivity after incubation with this rat kidney enzyme preparation according to radioimmunoassay using guinea pig antibody to bovine parathyroid hormone and <sup>125</sup>I-labeled highly purified bovine parathyroid hormone. Such activity of destroying PTH immunoreactivity, proportional to the amount of enzyme and duration of incubation, was lost after heating at 60°C for 10 min. The optimum pH, 8.6, and susceptibility to inhibitors such as p-chloromercuribenzoate, monoidoacetate, o-phenanthroline and EDTA were similar to those in the hydrolysis of <sup>125</sup>I-PTH.

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          Author and article information

          Horm Res Paediatr
          Hormone Research in Paediatrics
          S. Karger AG
          21 November 2008
          : 4
          : 4
          : 213-218
          Department of Geriatrics, University of Tokyo Faculty of Medicine, Tokio
          178310 Horm Res 1973;4:213–218
          © 1973 S. Karger AG, Basel

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          Pages: 6


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