Phosphorylation of chloride-ATPase reconstituted fromAplysia gut

Publisher Website
Google Scholar
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 Mg2+. In organic phosphate concentrations directly (Pi) enhanced phosphoprotein formation in the presence of increasing concentrations of Mg2+. It was also shown that the calculated rate constant for E1‐P formation was 26/sec. This approximated E1‐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.

This publication has 9 references indexed in Scilit: