Phosphorylation of chloride-ATPase reconstituted fromAplysia gut

✍ Scribed by Gerencser, George A. ;Zhang, Jianliang

• Book ID: 102334353
• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 93 KB
• Volume: 289
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1029

✦ Synopsis

Abstract

The present study was primarily done to compare cation‐ATPase phosphorylation kinetics with an anion‐ATPase’s phosphorylation kinetics because of the paucity of information in this area. Utilizing a proteolipsomal preparation containing Cl^–^‐ATPase from Aplysia gut, it was demonstrated that phosphorylation of this P‐type ATPase was absolutely dependent upon Mg^2+^. In organic phosphate concentrations directly (P~i~) enhanced phosphoprotein formation in the presence of increasing concentrations of Mg^2+^. It was also shown that the calculated rate constant for E~1~‐P formation was 26/sec. This approximated E~1~‐P rate constant values for other electrogenic, uniport P‐type ATPases, and therefore it was concluded from the results that the anion‐ATPase phosphorylation kinetics did not greatly differ from cation‐ATPase phosphorylation kinetics. J. Exp. Zool. 289:472–475, 2001. © 2001 Wiley‐Liss, Inc.