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欠压检测电路 UNDERVOLTAGE SENSING CIRCUIT
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Proceedings
of
the
National
Academy
of
Sciences
Vol.
66,
No.
4,
pp.
1190-1198,
August
1970
i-Galactoside
Transport
in
Bacterial
Membrane
Preparations:
Energy
Coupling
via
Membrane-Bound
D-Lactic
Dehydrogenase
Eugene
M.
Barnes,
Jr.*
and
H.
R.
Kabackt
NATIONAL
HEART
AND
LUNG
INSTITUTE,
NATIONAL
INSTITUTES
OF
HEALTH,
BETHESDA,
MARYLAND
Communicated
by
E.
R.
Stadtman,
May
19,
1970
Abstract.
The
transport
of
f3-galactosides
by
isolated
membrane
preparations
from
Escherichia
coli
strains
containing
a
functional
y
gene
is
markedly
stimu-
lated
by
the
conversion
of
D-lactate
to
pyruvate.
The
addition
of
D-lactate
to
these
membrane
preparations
produces
a
19-fold
increase
in
the
initial
rate
of
uptake
and
a
10-fold
stimulation
of
the
steady-state
level
of
intramembranal
lactose
or
thiomethylgalactoside.
Succinate,
DL-a-hydroxybutyrate,
and
L-
lactate
partially
replace
D-lactate,
but
are
much
less
effective;
ATP
and
P-enol-
pyruvate,
in
addition
to
a
number
of
other
metabolites
and
cofactors,
do
not
stimulate
lactose
transport
by
the
vesicles.
Lactose
uptake
by
the
membrane
preparations
in
the
presence
of
D-lactate
requires
oxygen,
and
is
blocked
by
electron
transport
inhibitors
and
proton
conductors;
however,
uptake
is
not
significantly
inhibited
by
high
concentrations
of
arsenate
or
oligomycin.
Fur-
thermore,
the
P-enolpyruvate-P-transferase
system
is
not
involved
in
,3-galacto-
side
transport
by
the
E.
coli
membrane
vesicles.
The
findings
indicate
that
the
3-galactoside
uptake
system
is
coupled
to
the
membrane-bound
D-lactic
dehydro-
genase
via
an
electron
transport
chain
but
does
not
involve
oxidative
phosphoryl-
ation.
Although
the
,3-galactoside
transport
system
of
Escherichia
coli
has
been
ex-
amined
in
very
great
detail,
the
mechanism
of
the
coupling
of
metabolic
energy
to
active
f3-galactoside
transport
remains
poorly
understood.
Scarborough,
Rumley,
and
Kennedy'
suggested
an
involvement
of
ATP
in
the
lactose
transport
system
of
E.
coli.
However,
recent
studies
by
Pavlasova
and
Harold2
on
anaero-
bic
methyl-l-thio-$-D-galactoside
(TMG)
uptake
indicate
that
uncouplers
of
oxidative
phosphorylation
block
TMG
accumulation
but
do
not
alter
ATP
levels.
Fox
and
Kennedy
demonstrated
the
existence
of
a
"permease"
protein
(the
M
protein)
which
was
a
product
of
the
y
gene.3
The
subsequent
suggestion
of
a
role
for
the
P-enolpyruvate-P-transferase
system
in
TMG
uptake4
in
E.
coli
raised
the
possibility
that
the
M
protein
might
be
an
inactivated
Enzyme
II.
This
topic
has
been
discussed
in
detail
in
a
recent
review.5
Recent
studies
in
this
laboratory
have
described
the
coupling
of
a
membrane-
bound
D-lactic
dehydrogenase
to
amino
acid
transport
in
isolated
membrane
preparations
from
E.
coli.6
This
paper
reports
a
similar
coupling
of
the
83-galac-
1190
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