Calf Intestinal Alkaline Phosphatase I. Improved Isolation Method and Molar Composition of the Purified Phosphatase
✍ Scribed by Plato Portmann; Andreas Jörg; Kurt Furrer; Hans-Sepp Walker; Peter Leuthard; Jean-François Sudan; FrançOis Perriard; Jean-François Comment; Geneviève Leva; Jean-pierre Nell
- Publisher
- John Wiley and Sons
- Year
- 1982
- Tongue
- German
- Weight
- 698 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
Abstract
A modified and improved method for isolation of calf intestinal alkaline phosphatase is described. By this method 300 to 400 mg of pure enzyme was prepared in a relatively short time. On the basis of the results of ultracentrifugation and of the free, polyacrylamide and immunoelectrophoresis the phosphatase obtained is found to be a homogenous glycoprotein, containing firmly bound zinc, magnesium and phosphoric acid. The molar composition of the enzyme and the catalytic activity were determined with different substrates and buffers.