FORMAL COMPLAINT - Sweden Confidential
FORMAL COMPLAINT - Sweden Confidential
FORMAL COMPLAINT - Sweden Confidential
You also want an ePaper? Increase the reach of your titles
YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.
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