1954_thomson_rhs_1528_1.pdf

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LSD No.63
(§102a)
L
121.2
cholinesterase
inhibition
THOMPSON,
R.H.S.,
TICKNER, A.,
WEBSTER,
G.R.
(Dept.of
Chem.Pathol., G_'s Hosp._ed.gchool, London)
C_ol_-Asterase
Lnhibition
by lveerwl¢
acid diethvlamide.
Biochem.J.58,xix(1954)
•
l.|tt[e
is
at
present
known
of biochemical
changes
that
may
accompany
the
psychological
effecta
produced
by administration
of lysergic
acid di.
ethylamide
to man.
The
action
of
this
com.
pound
on
a
number
of mammalian
esterases
hews
therefore
been studied.
It has been
shown
that
concentrations
of the order of 10-6M
cause
50 %
inhibition
of human
plasma
cholinesterase.
Tri-
butyrin
hydrolysis
by
human
plasma
is
inhibited
to
about
the same
degree.
On the other
hand
the
true cholinesterase
m human
erythrocytes
is not
mgnificantly
affeoted by 10 times the concentrat,_.
required to
produce
90
%
inhibition
of the
plasm_
enz_ne.
It has been shown
that this inhibition
of the
plasma cholinesterase
reversible.
Ps_,ldo-cholinestera_.
is competitive,
activitv
and is readily
in a number
of
di_rent
areas
of
the
h,.,,an
brain
m also
inhibited
capprox.
60 % by 5
×
)0-'
M).
As
in
the erytbrocytes,
true cholinesterase
in
the-brain
is
unaffected
by
these
concentrations.
Tributyrin
hydrolysis
by
brain
earlier
is
also
largely
unaffected,
oonfirmmg
observations
of Ord & Thompson
(1952)
the
that
pseudo-cholinesterase
in brain,
in
contrast
to that
in the
plasma,
does not contribute
to
any
significant
degree
to the
hydrolysis
of tributyrin
by this
tissue.
The
pseudo-cholinesterase
of
human
brain
appears
to be more sensitive
to inhibition
by LSD
than the corresponding
enzyme
in
the brains of the
other animal
species which we
},ave
studied.
Thus,
butyryleholine
hydrolysis
by
rat, guinea
pig and
chicken
brain
which produce
is hardly
affected
by concentrations
80-90
%
inhibition
in
human brain.
Rabbit
and
monkey
brain pseudo-cholinesterase
are
slightly
more
sensitive,
though
in
each case
considerably
less so than the
corresponding
enzyme
in
human brain.
REFERENCE
Ord, M. G.
&
Thompson,
245.
R.
H.
S. (1952).
Biochem. J.
51,
( 6993)
mfT/bh
llr_
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