The kinetic properties of a microsomal gill (Na(+),K(+))-ATPase from the blue crab Callinectes danae were analyzed using the substrate p-nitrophenylphosphate. The (Na(+),K(+))-ATPase hydrolyzed PNPP obeying cooperative kinetics (n=1.5) at a rate of V=125.4+/-7.5 U mg(-1) with K(0.5)=1.2+/-0.1 mmol
The contractures induced by 20-200 mM [K+]o in single crab muscle fibers were resolved into two components. The first component, consisting of single twitches or brief tetanic contractions, was associated with electrogenic membrane responses. The second occurred after spiking subsided with an
The kinetic properties of a microsomal gill (Na(+), K(+)) ATPase from the blue crab, Callinectes danae, acclimated to 15 per thousand salinity for 10 days, were analyzed using the substrate p-nitrophenylphosphate. The (Na(+), K(+))-ATPase hydrolyzed the substrate obeying Michaelian kinetics at a
The modulation by Na(+), K(+), NH(4)(+) and ATP of the (Na(+),K(+))-ATPase in a microsomal fraction from Callinectes danae gills was analyzed. ATP was hydrolyzed at high-affinity binding sites at a maximal rate of V=35.4+/-2.1 Umg(-1) and K(0.5)=54.0+/-3.6 nM, obeying cooperative kinetics
This investigation provides an extensive characterization of the modulation by ATP, Mg(2+), Na(+), K(+) and NH(4)(+) of a gill microsomal (Na(+),K(+))-ATPase from Callinectes danae acclimated to 15 per thousand salinity. Novel findings are the lack of high-affinity ATP-binding sites and a 10-fold
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