Mobile Phone Turns Enzyme Solution into A Gel

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14 Jan 2005 15:24:33 -0000

 

Mobile Phone Turns Enzyme Solution into A Gel

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ISIS Press Release 14/01/05

 

Mobile Phone Turns Enzyme Solution into A Gel

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A highly reproducible non-thermal effect of mobile phones

depends on interaction between protein and water. Dr. Mae-

Wan Ho says it brings us closing to understanding the

biophysics involved in how weak electromagnetic radiation

can have biological effects. Sources for this article are

posted on ISIS members' website

http://www.i-sis.org.uk/full/MPTESIGFull.php.

Details here http://www.i-sis.org.uk/membership.php

 

Serious brain damage unaccounted for

 

The most striking effect of exposure to the radio-frequency

(RF) radiation from mobile phones is damage to the brain and

brain cells of rats (see " Mobile phones & brain damage "

SiS24 http://www.i-sis.org.uk/isisnews/sis24.php), which

were found at levels of exposure far below the current

safety limits. After just two hours of such exposure, blood

albumin leaked into the brain causing brain cells to die;

and the effects lasted for at least 50 days after a single

exposure. But no clear mechanism has emerged to explain this

or other `non-thermal' effects of electromagnetic fields

(EMFs) even after a concerted, Europe-wide research

programme (see " Confirmed: mobile phones break DNA and

scramble genomes " , this series

http://www.i-sis.org.uk/CMPBDASG.php).

 

I have suggested that phase changes in cell water triggered

by EMFs may be involved in causing many biological effects,

but there has been a complete lack of support for research

in that area (see " Electromagnetic fields, leukaemia and DNA

damage " , SiS24 http://www.i-sis.org.uk/isisnews/sis24.php).

 

Now, new research findings make that suggestion a great deal

more plausible.

 

A `breakthrough' in identifying mechanisms?

 

Researchers at the University of Rome in Italy led by Mario

Barteri in the Chemistry Department report striking changes

in a solution of an enzyme after exposure to RF radiation

from mobile phones. This is the first time such a simple,

reproducible, in vitro system has been devised to study the

effects of EMFs.

 

The enzyme, acetylcholine esterase, involved in transmitting

nerve signals from the brain to the skeletal muscle, has

been purified and studied in great detail and commercial

preparations are readily available. The researchers chose to

study the acetylcholine esterase from the electric eel.

 

The enzyme was dissolved in a buffer solution in water and

identical samples were exposed to RF radiations within the

range of 915-1822 megahertz for 1 to 50 minutes, while the

control (unexposed) was wrapped securely in aluminium foil

to screen the RF radiations. A commercial cellular phone was

used as the source of RF radiation at a specific absorption

rate (SAR) of 0.51W/kg, with the mobile phone operating in

the receiving mode.

 

After exposing the enzyme solution, the researchers used a

range of physical measurement techniques to characterise the

changes.

 

First they passed the solutions down a gel filtration

column, which separates protein molecules by size. At short

irradiation times between 1 to 10 min, no difference from

the unexposed control was found; a single protein peak was

identified, representing the enzyme in its usual `dimeric'

form consisting of two protein units associated together.

However, after 20 min or more, a new peak was formed in

addition to the old; the new peak representing the monomeric

or dissociated form of the protein. This profile remained

stable after one day at room temperature, showing that

irreversible change had taken place in the solution.

 

Measurements on the rate constants of the enzyme activity

similarly indicated that up to 10 min of RF radiation

exposure had no effect, but after 20 min or more, the rate

constants changed dramatically, which was consistent with

previous findings from another laboratory reporting increase

in the enzyme activity in mice after twenty minutes exposure

to mobile phone radiation.

 

This change in the kinetic properties of the enzyme was

apparently not accompanied by change in the three-

dimensional shape (conformation) of the protein, at least as

measured by circular dichroism (a technique for

characterising the shape of molecules based on measuring the

unequal absorption of right and left plane-polarized light).

 

Measurement by X-ray scattering, however, revealed a drastic

change in the collective organisation of the protein in

solution, which suggested that a phase of `hydrogel' had

separated out from the main solution. This hydrogel was made

up of monomeric protein molecules associated with lots of

water molecules to form a collective phase.

 

Finally, the researchers took a scanning electron micrograph

of the control and the exposed sample, which showed up the

marked difference. The native, unexposed sample appeared as

a random suspension of enzyme molecules; whereas the

irradiated sample appeared as a highly oriented sample with

a regular periodic pattern.

 

RF radiation trigger interaction of enzyme protein with

water

 

The enzyme protein has a very strong negative charge near

the entrance to the `gorge' containing the active site

(where the substrate is bound), which gives a strong dipole

(separated positive and negative electric charges) oriented

along gorge. This makes the protein sensitive to

fluctuations of the electric field generated by the RF

radiation from the cellular phone; which in turn perturbs

the dipoles of the water molecules, resulting in the

formation of the hydrogel.

 

As a further check, the researchers carried out nuclear

magnetic resonance (NMR) measurements on the proton spin

relaxation times (T1) of the water molecules. For bulk

water, the relaxation time was 2983+27; for native enzyme

dissolved in water, it was 470+25; for enzyme exposed to RF

radiation for 20 min, it was 260+32, and exposed for 50 min,

220+38. The results, once again, are consistent with the

increased interaction of enzyme protein with water molecules

that one would find in a hydrogel.

 

The researchers said, rightly, that the results " cannot be

used to conclude whether exposure to RF during the use of

cellular phone can lead to any hazardous health effect " ; but

" they may be a significant model to verify these effects on

other biological systems. "

 

I believe however that these results are important in

contributing to our understanding of `non-thermal' effects:

they are mediated through the collective structure of water,

especially as conceived by a number of key researchers in

biological water.

 

Collective structure of water important

 

The phenomena observed by Barteri and co-workers depend on

the collective structure of water, which effectively sums

and amplifies the effect of weak EMFs. It provides the

mechanism for non-thermal effects that conventional

scientists find so " inconceivable " , largely out of

ignorance.

 

The results also appear to be consistent with the work of

researchers who made pioneering discoveries on water in the

cell. Gilbert Ling, in particular, first proposed that water

molecules form polarised multi-layers over extended protein

surfaces inside the cells (see " Strong medicine for cell

biology " SiS 24 http://www.i-sis.org.uk/isisnews/sis24.php).

This proposal received remarkable confirmation recently in

an in vitro system (see " Water forms massive exclusion

zones " , SiS23 http://www.i-sis.org.uk/isisnews/sis23.php)

and in the cell (see " What's the cell really like? " SiS24

http://www.i-sis.org.uk/isisnews/sis24.php); and is also

consistent with findings in my own laboratory that the water

in living organisms is an intrinsic part of the liquid

crystalline continuum of the body (see The Rainbow and the

Worm, the Physics of Organisms

http://www.i-sis.org.uk/rnbwwrm.php).

 

The hydrogel created by Barteri and

colleagues after exposing the enzyme solution to RF

radiation are very likely to consist of multilayers of

polarised water molecules on extended protein surfaces. The

RF radiation acts as a trigger to dissociate the protein

dimers into monomers and to interact with water; without

however, destroying enzyme activity; if anything it appeared

to have increased enzyme activity. The findings of Barteri's

team are also consistent with the proposals of Martin

Chaplin and Frank Mayer, that water switches between a low-

density and a high-density phase with very different

interactions between proteins and water molecules that

change enzyme activities and cell function (see " the

importance of cell water " and " What's the bacterium really

like? " , SiS24 http://www.i-sis.org.uk/isisnews/sis24.php).

Martin Chaplin expresses surprise at the result, as did the

authors of the research paper. " The jellification would seem

to be very specific to the properties of that particular

enzyme. The process by which the radiation increases the

hydration of the protein and causes its dissociation can be

explained, but [is possibly] an extreme case of what can

occur. " He adds, " The work does show how the power of water

to hydrate molecules increases when the `normal' hydrogen

bonding is disrupted; and also that the change in hydration

may not be readily reversible. I doubt if any present

computer model of water could reproduce this phenomenon. " We

can no longer accept the mantra that there is no

" conceivable " mechanism that could explain non-thermal

effects of EMFs, and that the current EMF exposure limits

may well be harmful.

 

 

 

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