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Last Updated: 2 years ago

Possible Interaction: Tryptophan and Vitamin B 6

supplement:

Tryptophan

supplement:

Vitamin B 6

Research Papers that Mention the Interaction

We believe that the metabolic alteration of tryptophan is secondary to a deficit of pyridoxal phosphate and nicotinamide-dependent enzyme activities.
Acta vitaminologica et enzymologica  •  1975  |  View Paper
6 Tryptophan loading was followed by an abnormally large increase in the excretion of these and other metabolites, which could be partially blocked by the simultaneous administration of pyridoxine , suggesting that there may be a functional deficiency of pyridoxine.
Seminars in arthritis and rheumatism  •  1973  |  View Paper
Since pyridoxine is required for orderly catabolism of tryptophan and pyridoxine corrected this metabolic aberration, it is not unreasonable to state that in hyperthyroidism, the availability of pyridoxine is limited.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine  •  1960  |  View Paper
However, these two infants, like the control infants, required only 0.3 to 0.4 mg of vitamin B6 daily to prevent excretion of xanthurenic acid after receiving a dose of tryptophan.
Pediatrics  •  1957  |  View Paper
Thus, both tryptophan and pyridoxine possess antihypertensive properties, and the combination of the two appeared to provide greater protection than either alone.
Pharmacology  •  1995  |  View Paper
Larger decreases in the catabolism of tryptophan were seen after pyridoxine deprivation.
Archives of biochemistry and biophysics  •  1985  |  View Paper
It is suggested that this increase in the uptake of tryptophan into the brain following a relatively large dose of vitamin B6 may explain the beneficial action of the vitamin in some cases of depressive illness.
Journal of neurochemistry  •  1984  |  View Paper
It appeared that a high dose of tryptophan in B-6-deficient rats could cause a greater deficiency of pyridoxal 5-phosphate.
The Biochemical journal  •  1984  |  View Paper
Steady-state fluorescence spectra gave tryptophan emission of the apoenzyme that is 3.3-fold higher than the emission of either the native or reconstituted enzyme, suggesting that PLP is a potent quencher of tryptophan emission.
Archives of biochemistry and biophysics  •  2009  |  View Paper
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