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FORMAL COMPLAINT - Sweden Confidential

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United Nations petition — incomplete report<br />

attributable to perphenazine/Trilafon/Fentazine, as I believe this may be of<br />

common interest and value —<br />

Firstly perphenazine will overturn and largely invalidate the endogenous pro-<br />

duction, chemical properties and natural distribution etc of several catechol-<br />

amines chiefly generated by hydroxylation of the L-isomeric amino acid<br />

tyrosine* (*cf tyrosinase → cathecol oxidase).<br />

The 3,4-dihydroxyphenylalanine* (*DOPA) formed by the tyrosine hydroxylase<br />

is the biosynthetic precursor of the essential cathecholamines dopamine* (*[3,4-<br />

dihydroxyphenyl]ethyl amine), noradrenaline* (*norepinephrine) and<br />

adrenaline* (*epinephrine).<br />

The cathecolamines serves and triggers an impressive number specialized<br />

physiological and neurochemical etc functions and actions impeded by the<br />

toxicological impact of perphenazine; vital mechanisms regulating e.g blood<br />

pressure, heart rate, breathing, metabolism and muscle tone are temporary or<br />

permanently corrupted/destroyed. Dangerously interfering with the hydroxy-<br />

lation of phenylalanine to tyrosine and subsequent dihydropteridine reductase,<br />

the transamination of tyrosine to p-hydroxyphenylpyruvate and concurrent<br />

reaction with O2 to form homogentisate is significantly incapacitated, thus<br />

provoking detrimental accumulation of the nerve poison phenylpyruvic acid in<br />

the body fluids as well as in varietal tissues where it evades most drug<br />

monitoring and toxicological screening procedures usw. Exerting a generally<br />

cytopathogenic effect, perphenazine obstructs the natural interaction between<br />

various nitrogenase and reductase agents, and consequently upset the entire<br />

nitrogen<br />

equilibrium/metabolism; hydrolysis of ATP* (*adenosine triphosphate) and<br />

hepatic amino acid degradation is incapacitated, and the constructive functions<br />

of v.g the enzymes alanine/aspartate aminotransferase and glutamate dehydro-<br />

genase perilously hampered.<br />

Whereas practically all fundamental properties of cells are products of molecular<br />

interactions between their respective nucleic acids and proteins, the metabolically<br />

decisive amounts of the adenine nucleotides ATP/ADP/AMP is relatively<br />

disproportionated by the principally cytoclastic influence waged by perphenazine<br />

— ATPs phosphoryl transfer potential is diminished, and efficient hydro-<br />

lysis of phosphocreatine obstructed.<br />

Adenosine triphosphate is the universal main carrier of all forms of chemical<br />

energy in living organisms — as it transfer energy to other molecules, ATP loses<br />

its terminal phosphate group as inorganic phosphate* (*orthophosphate, Pi), or<br />

two of its phosphate groups as inorganic pyrophosphate* (*PPi), becoming<br />

adenosine diphosphate* (*ADP) or adenosine monophosphate* (*AMP), respectively.<br />

Described hydroxylation of ATP to ADP/Pi and AMP/PPi relies on the catalytic<br />

purveyance of the enzymes hexokinase* (*catalyzing the phosporylation of glu-<br />

90<br />

<strong>FORMAL</strong> <strong>COMPLAINT</strong> VS THE KINGDOM OF NORWAY<br />

by Wilh. Werner WINTHER, Norway<br />

90

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