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The Airpax™ SNAPAK® series is a snap-acting hydraulic-magnetic circuit protector that combines power switching and accurate, reliable circuit protection in one aesthetically pleasing package. The SNAPAK® combines the functions of three separate components: power switch, fuse and fuse holder. To the OEM, this means that only one item has to be mounted instead of three. Less assembly is required, inventory is cut by two-thirds and greater panel density is obtainable with less clutter.
In addition, the SNAPAK® can be operated at either DC or 50/60Hz, eliminating the need to specify, order and stock separate units.
The Mg 2+ dependence of the kinetics of the phosphorylation and conformational changes of Na +,K +-ATPase was investigated via the stopped-flow technique using the fluorescent label RH421. The enzyme was preequilibrated in buffer containing 130 mM NaCl to stabilize the E1(Na +) 3 state. On mixing with ATP, a fluorescence increase was observed. Two exponential functions were necessary to fit the data. Both phases displayed an increase in their observed rate constants with increasing Mg 2+ to saturating values of 195 (± 6) s −1 and 54 (± 8) s −1 for the fast and slow phases, respectively. The fast phase was attributed to enzyme conversion into the E2MgP state.
The slow phase was attributed to relaxation of the dephosphorylation/rephosphorylation (by ATP) equilibrium and the buildup of some enzyme in the E2Mg state. Taking into account competition from free ATP, the dissociation constant ( K d) of Mg 2+ interaction with the E1ATP(Na +) 3 state was estimated as 0.069 (± 0.010) mM.
This is virtually identical to the estimated value of the K d of Mg 2+-ATP interaction in solution. Within the enzyme-ATP-Mg 2+ complex, the actual K d for Mg 2+ binding can be attributed primarily to complexation by ATP itself, with no apparent contribution from coordination by residues of the enzyme environment in the E1 conformation. Introduction An important role of Mg 2+ in biology is as a cofactor of ATP. The Mg 2+ ion is complexed by the negatively charged oxygens of its phosphate groups.
The Mg 2+ is thus thought to help shield the negative charges of the phosphates, allowing reaction with the electron pairs of attacking groups and facilitating phosphoryl transfer (). One of the most important enzymes in which this is the case is the Na +,K +-ATPase, which is responsible for maintaining electrochemical potential gradients for Na + and K + across the plasma membrane. To our knowledge, no crystal structure of the Na +,K +-ATPase in the E1 state with bound Mg 2+ and ATP has yet been reported. Nadpisi dlya ugolkov syuzhetno rolevih. Nevertheless, based on a published crystal structure of the related enzyme sarcoplasmic reticulum Ca 2+-ATPase (), and using computer modeling, Patchornik et al.
() suggested that, like the phosphates of ATP, the aspartate residues D710, D443, and D714 contribute to Mg 2+ coordination. Although this may be correct, it is difficult from crystal structural data to make conclusions about the relative strengths of interactions. The aim of this article is to provide reliable experimental data on the strength of binding of Mg 2+ ions to the Na +,K +-ATPase. A difficulty in studying Mg 2+ interaction with the Na +,K +-ATPase under physiological conditions, i.e., in the presence of ATP and Na + ions, is that it immediately induces phosphorylation, so that Mg 2+ binding cannot be separated from the phosphorylation reaction. This precludes equilibrium binding studies. Here we have, therefore, applied a pre-steady-state kinetic technique (stopped-flow spectrofluorimetry) utilizing the voltage-sensitive fluorescent probe RH421.