Effect of low frequency, low amplitude magnetic fields on the permeability of cationic liposomes entrapping carbonic anhydrase II. No evidence for surface enzyme involvement (Articolo in rivista)

Type
Label
  • Effect of low frequency, low amplitude magnetic fields on the permeability of cationic liposomes entrapping carbonic anhydrase II. No evidence for surface enzyme involvement (Articolo in rivista) (literal)
Anno
  • 2000-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/1521-186X(200010)21:7<499::AID-BEM3>3.0.CO;2-9 (literal)
Alternative label
  • Ramundo-Orlando, A; Mattia, F; Palombo, A; D'Inzeo, G (2000)
    Effect of low frequency, low amplitude magnetic fields on the permeability of cationic liposomes entrapping carbonic anhydrase II. No evidence for surface enzyme involvement
    in Bioelectromagnetics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ramundo-Orlando, A; Mattia, F; Palombo, A; D'Inzeo, G (literal)
Pagina inizio
  • 499 (literal)
Pagina fine
  • 507 (literal)
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  • 21 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Sapienza University Rome; Consiglio Nazionale delle Ricerche (CNR) (literal)
Titolo
  • Effect of low frequency, low amplitude magnetic fields on the permeability of cationic liposomes entrapping carbonic anhydrase II. No evidence for surface enzyme involvement (literal)
Abstract
  • Observations recently reported by our group indicate that combined 7 Hz sinusoidal (B-acpeak = 50 mu T) and parallel static (B-dc = 50 mu T) magnetic fields can induce a significant increase in diffusion rate of substrate across carbonic anhydrase (CA)-loaded liposomes (DPPC:Chol:SA). A direct involvement of charges of stearylamine (SA) on the lipid membrane surface was also demonstrated. Kinetic studies showed that CA. was mainly entrapped in Liposomes at 5:3:2 molar ratio, although a small amount (17%) of enzyme was also located on the external surface of these cationic liposomes. In this paper we report steady state kinetic studies on this latter CA after ELF-EMFs exposure. No difference in the apparent K-m between exposed and sham samples was observed. On the contrary the apparent V-max was increased by approximately a factor of 2 after field exposure. In spite of the proteolytic digestion of this external CA, a significant increase of enzymatic activity, as a function of increase in the diffusion rate of substrate across the lipid bilayer, was observed in the exposed samples. Based on these results, a conformational change induced by the field on the CA located on the external surface of 5:3:2 liposomes is excluded as an explanation for our previous observations, supporting the primary role of bilayer SA in the interaction with ELF A model of ELF interaction, based on the Larmor precession theory, explaining the physical phenomenon induced on the dipole of SA has been developed. (C) 2000 Wiley-Liss, Inc. (literal)
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