title: New experimental technique for detecting the effect of low-frequency electric fields on enzyme structure.
abstract: 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 phosphatase. The enzyme was exposed to a 50-Hz current at different densities (10 to 60 mA/cm2 rms) or to a sinusoidal or square-wave current at an average density of 3 mA/cm2 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.
authors.affiliation: Dipartimento di Ingegneria Chimica, Universita di Napoli, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Greco
authors.forename: L
authors.initials: L
authors.lastname: Gianfreda
authors.forename: G
authors.initials: G
authors.lastname: d'Ambrosio
authors.forename: R
authors.initials: R
authors.lastname: Massa
authors.forename: A
authors.initials: A
authors.lastname: Scaglione
authors.forename: M R
authors.initials: MR
authors.lastname: Scarfi
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism / Q000528:radiation effects*; D004574:Electromagnetic Fields; D055590:Electromagnetic Phenomena; D004795:Enzyme Stability; D011487:Protein Conformation / Q000528:radiation effects; D011846:Radio Waves
chemical_list: D000135:Acid Phosphatase