Abstract:
The kinetic properties of Na+, K+-ATPase from different lobes of swiss albino
mice brain were studied under conditions of enzyme saturation with Mg-ATP
(0.25-10 mM). By participating in the regulation of ion and voltage gradients, the
Na-K pump (Na+, K+-ATPase) influences many aspects of cellular physiology.
The apparent Michaelis constant (Km) (Mm) and the apparent maximum velocity
(Vmax) (n mol Pi min-1 mg protein) for mice brain lobes Bl-B5 were as follows
(0.57; 616), (1.45; 848), (8.44; 7634), (3.19; 95) and (3.34; 110), respectively.
The specific activity of lobe B3 has the highest followed by B2, B1, B5 and B4 in
decreasing order of activity. It seems that each brain lobe has its own Michaelis
constant (Km) and maximum velocity (Vmax) that is needed for their own
physiological role. Differences in kinetic properties of Na, K-ATPase from
different brain lobes may be due to the isoenzyme diversity and adaptations to
specific physiological demands of the specific brain regions.
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