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Department of Medical Physiology, The Panum Institute, University of Copenhagen, DK-2200 Copenhagen; and Department of Internal Medicine, Køge Hospital, DK-4600 Koge, Denmark
Influx of
D-aspartate
(D-Asp),
L-glutamate
(L-Glu), and serine (Ser) across
the brush-border membrane of the intact mucosa from rabbit ileum has
been examined. L-Glu influx is
chloride independent and completely sodium dependent.
D-Asp and
L-Glu share a transport system
with a maximum transport rate of 1 µmol · cm
2 · h
1
and an apparent affinity constant
(K1/2) of
~0.3 mM. The function of this transport system is pH insensitive
between pH 5.65 and 8.2, and bipolar amino acids do not affect the way
in which the transport system handles
D-Asp and
L-Glu. The characteristics of
this transport system match those of system
X
AG. L-Glu and Ser share a
transporter for which the inhibitor constant (Ki) of
L-Glu against Ser decreases from
54 to 10 mM when pH is reduced from 7.2 to 5.65, while the maximum rate
of transport remains unaffected at ~10
µmol · cm
2 · h
1.
The Ki values (5 mM) of Ser against L-Glu influx
and the L-Glu-sensitive contribution to Ser influx (0.8 µmol · cm
2 · h
1
at 1 mM Ser) are the same at both pH values. The
L-Glu-sensitive transport of Ser
together with the contribution of system
bo,+ account for ~50% of Ser
influx at pH 7.2. The remaining 50% can be ascribed to system B. Transport of Ser by system B is reduced by >95% at pH 5.65. At pH
7.2 Ki of Ser
against transport of leucine (Leu) by system B is 18 mM and
Ki of Leu against
transport of Ser is 1.7 mM. The low-affinity transport of
L-Glu and the
L-Glu-sensitive transport of Ser
are performed by an equivalent of system ASC. Supplementary experiments
using the jejunum confirm the validity of these results for a major
portion of the rabbit small intestine.
anionic amino acids; biological transport; amino acids; brush-border membrane; intestine
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