Premium
New experimental technique for detecting the effect of low‐frequency electric fields on enzyme structure
Author(s) -
Greco Guido,
Gianfreda Liliana,
d'Ambrosio Guglielmo,
Massa Rita,
Scarfi Maria Rosaria,
Scaglione Antonio
Publication year - 1990
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/bem.2250110108
Subject(s) - dipole , electric field , square wave , enzyme , electric current , low frequency , chemistry , current (fluid) , kinetic energy , current density , perturbation (astronomy) , electric dipole moment , materials science , molecular physics , chemical physics , biophysics , nuclear magnetic resonance , physics , thermodynamics , voltage , classical mechanics , biochemistry , organic chemistry , biology , quantum mechanics , astronomy
A new experimental approach has been developed to determine kinetic and thermodynamic parameters of the inactivation of an enzyme under labile conditions both with and without exposure to electrical currents as sources of perturbation. Studies were undertaken to investigate if low‐frequency electric currents can accelerate the thermal inactivation of an enzyme through interactions with dipole moments in enzymatic molecules and through related mechanical stresses. The experiments were conducted with the enzyme acid posphatase. The enzyme was exposed to a 50‐Hz current at different densities (10 to 60 mA/cm 2 rms) or to a sinusoidal or square‐wave current at an average density of 3 mA/cm 2 and frequencies from, respectively, 50 Hz to 20 kHz and 500 pulses per second (pps) to 50,000 pps. Positive‐control experiments were performed in the presence of a stabilizer or a deactivator. The results indicate that the technique is sensitive to conformational changes that otherwise may be impossible to detect. However, exposure to electric currents under the experimental conditions described herein showed no effects of the currents.