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/lp/karger/further-characterization-of-alkaline-phosphatases-of-human-kidney-and-SkmeRq5mxi
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- Publisher
- Karger
- Copyright
- © 1977 S. Karger AG, Basel
- ISSN
- 1018-2438
- eISSN
- 1423-0097
- DOI
- 10.1159/000231841
- Publisher site
- See Article on Publisher Site
Abstract
Human kidney alkaline phosphatase (AP) react with antisera to liver and intestinal AP. The respective kidney enzymes are designated as K<sup>Li</sup> and K<sup>I</sup>. Comparison with liver AP showed that K<sup>Li</sup> was salted out at the same ammonium sulfate concentration (66%) as the liver enzyme; K<sup>Li</sup> was antigenically identical with liver AP; the electrophoretic mobility of K<sup>Li</sup> was that of a γ-globulin whereas liver AP was an α<sub>2</sub>-globulin. The liver enzyme was lighter (130,000 daltons) than K<sup>Li</sup> (150,000 daltons). K<sup>I</sup> and intestinal AP shared most properties: antigenically they were indistinguishable; both contained two components one of which was 80,000 daltons, the other was heavier (120,000 daltons for K<sup>I</sup>, 130,000 daltons for intestinal AP). Urinary AP consisted only of the lighter component (80,000 dalton). Methods for partial separation of the three kidney APs are given.
Journal
International Archives of Allergy and Immunology – Karger
Published: Jan 1, 1977