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ON THE MECHANISM OF TAURINE TRANSPORT AT BRAIN CELL MEMBRANES
Author(s) -
Lähdesmäkt P.,
Oja S. S.
Publication year - 1973
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1973.tb00253.x
Subject(s) - taurine , hypotaurine , cysteic acid , chemistry , membrane , biophysics , membrane transport , biochemistry , amino acid , biology , enzyme , cystine , cysteine
One non‐saturable and two saturable transport systems were demonstrated for taurine in rat brain slices. One of the saturable systems, designated β, is characterized by a high asnity for taurine and a low transport capacity, while the other, designated ω, by a low affinity and a high transport capacity. 2,4‐Dinitrophenol inhibited the saturable transport of taurine non‐competitively, while hypotaurine. β‐alanine, γ‐aminobutyric acid, N ‐methyl‐taurine and L‐cysteic acid inhibited transport competitively. It is thus inferred that the hypothetical carrier sites of taurine at cell membrane recognize to an equal degree strongly ionized electropositive and electronegative ends of an acceptable molecule separated by two or three carbon atoms. Two is the minimal and also the optimal carbon chain length in an acceptable molecule.