Synergistic stimulation by potassium and ammonium of K(+)-phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: novel property of a primordial pump

Arch Biochem Biophys. 2013 Feb 15;530(2):55-63. doi: 10.1016/j.abb.2012.12.006. Epub 2012 Dec 19.

Abstract

We provide an extensive characterization of the modulation by p-nitrophenylphosphate, Mg²⁺, Na⁺, K(+), Rb⁺, NH(4)(+) and pH of gill microsomal K⁺-phosphatase activity in the posterior gills of Callinectes ornatus acclimated to low salinity (21‰). The synergistic stimulation by K⁺ and NH(4)(+) of the K⁺-phosphatase activity is a novel finding, and may constitute a species-specific feature of K(+)/NH(4)(+) interplay that regulates crustacean gill (Na⁺, K⁺)-ATPase activity. p-Nitrophenylphosphate was hydrolyzed at a maximum rate (V) of 69.2 ± 2.8nmolPimin⁻¹mg⁻¹ with K(0.5)=2.3 ± 0.1mmolL(-1), obeying cooperative kinetics (n(H)=1.7). Stimulation by Mg²⁺ (V=70.1 ± 3.0nmolPimin⁻¹mg⁻¹, K(0.5)=0.88 ± 0.04mmolL⁻¹), K⁺ (V=69.6 ± 2.7nmolPimin⁻¹mg⁻¹, K(0.5)=1.60 ± 0.07mmolL⁻¹) and NH(4)(+) (V=90.8 ± 4.0nmolPimin⁻¹mg⁻¹, K(0.5)=9.2 ± 0.3mmol L⁻¹) all displayed site-site interaction kinetics. In the presence of NH(4)(+), enzyme affinity for K⁺ unexpectedly increased by 7-fold, while affinity for NH(4)(+) was 28-fold greater in the presence than absence of K⁺. Ouabain partially inhibited K⁺-phosphatase activity (K(I)=320 ± 14.0μmolL⁻¹), more effectively when NH(4)(+) was present (K(I)=240 ± 12.0μmolL⁻¹). We propose a model for the synergistic stimulation by K⁺ and NH(4)(+) of the K⁺-phosphatase activity of the (Na⁺, K⁺)-ATPase from C. ornatus posterior gill tissue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonia / agonists
  • Ammonia / chemistry*
  • Ammonia / metabolism
  • Animals
  • Arthropod Proteins / chemistry*
  • Arthropod Proteins / metabolism
  • Brachyura / enzymology*
  • Gills / enzymology*
  • Kinetics
  • Microsomes / enzymology*
  • Nitrophenols / chemistry
  • Organophosphorus Compounds / chemistry
  • Potassium / agonists
  • Potassium / chemistry*
  • Potassium / metabolism
  • Salinity
  • Sodium-Potassium-Exchanging ATPase / chemistry*
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Arthropod Proteins
  • Nitrophenols
  • Organophosphorus Compounds
  • nitrophenylphosphate
  • Ammonia
  • Sodium-Potassium-Exchanging ATPase
  • Potassium