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Na,K‐ATPase function in alternating electric fields 1
Author(s) -
Blank Martin
Publication year - 1992
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.6.7.1314204
Subject(s) - ouabain , chemistry , ion , atpase , biophysics , ionic bonding , enzyme , extracellular , electric field , ion transporter , ion pump , range (aeronautics) , enzyme assay , analytical chemistry (journal) , sodium , biochemistry , physics , materials science , biology , chromatography , organic chemistry , quantum mechanics , composite material
Alternating currents affect ion transport processes and ATP splitting through changes in the activation of the membrane Na,K‐ATPase. Both processes vary with the frequency, and the effective range includes the environmental 60 Hz. ATP splitting by Na,K‐ATPase suspensions decreases for the enzyme under normal conditions, with the maximum effect at 100 Hz. ATP splitting increases when the enzyme activity is lowered to less than half its optimal value by changes in temperature, ouabain concentration, etc. These observations can be explained by the effects of the ionic currents on ion binding at the enzyme activation sites. Such a mechanism could account for the effects of electromagnetic fields on cells, as the transmembrane enzyme can convey the effect of an extracellular signal into the cell via ionic fluxes, and the measured threshold field is within the range of reported biological effects.—Blank, M. Na,K‐ATPase function in alternating electric fields. FASEB J. 6: 2434‐2438; 1992.