The Calf Intestinal Alkaline Phosphatase. II. Reaction between the metal content and the enzyme activity

✍ Scribed by Plato Portmann; Hubert Schaller; Geneviève Leva; Werner Venetz; Thomas Müller

• Book ID: 102252850
• Publisher: John Wiley and Sons
• Year: 1983
• Tongue: German
• Weight: 470 KB
• Volume: 66
• Category: Article
• ISSN: 0018-019X
• DOI: 10.1002/hlca.19830660320

✦ Synopsis

Abstract

Pure alkaline phosphatase (EC 3.1.3.1; 1500 U/mg) was dialyzed at 4° during 168 h against water, 10^−4^M EDTA or 10^−4^M o‐phenanthroline. During the dialysis, samples were periodically removed and analyzed for metal content and activity. The results indicate that 1 mol of native calf intestinal alkaline phosphatase contains 4 g‐atom of zinc and 4 g‐atom of magnesium tightly bound, and that both metal ions are necessary for full enzyme activity. The dialyzed, partially demetallized enzyme could be reactivated by the addition of zinc and/or magnesium salts.