Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding.

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Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding. / Takada, A; Grdisa, M; Diksic, M; Gjedde, A; Yamamoto, Y L.

In: Neurochemistry International, Vol. 23, No. 4, 1993, p. 351-9.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Takada, A, Grdisa, M, Diksic, M, Gjedde, A & Yamamoto, YL 1993, 'Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding.', Neurochemistry International, vol. 23, no. 4, pp. 351-9.

APA

Takada, A., Grdisa, M., Diksic, M., Gjedde, A., & Yamamoto, Y. L. (1993). Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding. Neurochemistry International, 23(4), 351-9.

Vancouver

Takada A, Grdisa M, Diksic M, Gjedde A, Yamamoto YL. Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding. Neurochemistry International. 1993;23(4):351-9.

Author

Takada, A ; Grdisa, M ; Diksic, M ; Gjedde, A ; Yamamoto, Y L. / Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding. In: Neurochemistry International. 1993 ; Vol. 23, No. 4. pp. 351-9.

Bibtex

@article{16120b60b31511debc73000ea68e967b,
title = "Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding.",
abstract = "We estimated constants for the binding of tryptophan (Trp) to plasma proteins, and for the transfer of Trp from plasma to brain in rat. The measurements were made under conditions in which the plasma and brain concentrations of Trp were raised to new steady-states for at least 10 min before being measured. The concentration of other competing amino acids were also at a steady-state. The plasma Trp concentration was elevated by i.p. injection of different doses of L-tryptophan methyl ester 60 min before the measurement of the plasma-brain transfer. We simultaneously measured blood flow with [14C]-butanol, and the brain tissue Trp uptake with [3H]Trp. The maximal velocity (Vmax), apparent half-saturation Michaelis-Menten constant (Km(app)), and diffusion constant (PdS) for Trp transport from plasma into brain were found to be 7.0 +/- 2.1 nmol g-1 min-1, 36 +/- 17 microM, and 0.065 +/- 0.006 ml g-1 min-1, respectively. The maximum plasma protein binding (Bmax) and dissociation constant (KD) for Trp were estimated at 360 +/- 16 nmol/ml-plasma and 81 +/- 10 microM, respectively. We conclude that the plasma protein binding of Trp inhibits the blood-brain transfer in inverse proportion to the plasma free Trp concentration.",
author = "A Takada and M Grdisa and M Diksic and A Gjedde and Yamamoto, {Y L}",
year = "1993",
language = "English",
volume = "23",
pages = "351--9",
journal = "Neurochemistry International",
issn = "0197-0186",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Rapid steady-state analysis of blood-brain transfer of L-Trp in rat, with special reference to the plasma protein binding.

AU - Takada, A

AU - Grdisa, M

AU - Diksic, M

AU - Gjedde, A

AU - Yamamoto, Y L

PY - 1993

Y1 - 1993

N2 - We estimated constants for the binding of tryptophan (Trp) to plasma proteins, and for the transfer of Trp from plasma to brain in rat. The measurements were made under conditions in which the plasma and brain concentrations of Trp were raised to new steady-states for at least 10 min before being measured. The concentration of other competing amino acids were also at a steady-state. The plasma Trp concentration was elevated by i.p. injection of different doses of L-tryptophan methyl ester 60 min before the measurement of the plasma-brain transfer. We simultaneously measured blood flow with [14C]-butanol, and the brain tissue Trp uptake with [3H]Trp. The maximal velocity (Vmax), apparent half-saturation Michaelis-Menten constant (Km(app)), and diffusion constant (PdS) for Trp transport from plasma into brain were found to be 7.0 +/- 2.1 nmol g-1 min-1, 36 +/- 17 microM, and 0.065 +/- 0.006 ml g-1 min-1, respectively. The maximum plasma protein binding (Bmax) and dissociation constant (KD) for Trp were estimated at 360 +/- 16 nmol/ml-plasma and 81 +/- 10 microM, respectively. We conclude that the plasma protein binding of Trp inhibits the blood-brain transfer in inverse proportion to the plasma free Trp concentration.

AB - We estimated constants for the binding of tryptophan (Trp) to plasma proteins, and for the transfer of Trp from plasma to brain in rat. The measurements were made under conditions in which the plasma and brain concentrations of Trp were raised to new steady-states for at least 10 min before being measured. The concentration of other competing amino acids were also at a steady-state. The plasma Trp concentration was elevated by i.p. injection of different doses of L-tryptophan methyl ester 60 min before the measurement of the plasma-brain transfer. We simultaneously measured blood flow with [14C]-butanol, and the brain tissue Trp uptake with [3H]Trp. The maximal velocity (Vmax), apparent half-saturation Michaelis-Menten constant (Km(app)), and diffusion constant (PdS) for Trp transport from plasma into brain were found to be 7.0 +/- 2.1 nmol g-1 min-1, 36 +/- 17 microM, and 0.065 +/- 0.006 ml g-1 min-1, respectively. The maximum plasma protein binding (Bmax) and dissociation constant (KD) for Trp were estimated at 360 +/- 16 nmol/ml-plasma and 81 +/- 10 microM, respectively. We conclude that the plasma protein binding of Trp inhibits the blood-brain transfer in inverse proportion to the plasma free Trp concentration.

M3 - Journal article

C2 - 8220177

VL - 23

SP - 351

EP - 359

JO - Neurochemistry International

JF - Neurochemistry International

SN - 0197-0186

IS - 4

ER -

ID: 14944398