Can nutrient supplements modify brain function? Am J Clin Nutr. The effects of acute and prolonged CRAM supplementation on reaction time and subjective measures of focus and alertness in healthy college students. J Int Soc Sports Nutr. Nelson Textbook of Pediatrics, 19th ed. Philadelphia, PA: Saunders Elsevier; Tyrosine supplementation mitigates working memory decrements during cold exposure.
Physiol Behav. Melmed: Williams Textbook of Endocrinology, 12th ed. Meyers S. Use of neurotransmitter precursors for treatment of depression.
Altern Med Rev. Parry BL. The role of central serotonergic dysfunction in the aetiology of premenstrual dysphoric disorder: therapeutic implications. CNS Drugs. Poustie VJ, Rutherford P. Tyrosine supplementation for phenylketonuria.
Cochrane Database Syst Rev. Richeldi L, et al. Efficacy of a tyrosine kinase inhibitor in idiopathic pulmonary fibrosis. N Engl J Med. New England maternal PKU project: prospective study of untreated and treated pregnancies and their outcomes. J Pediatr ; : — 8. Tyrosine supplementation in the treatment of maternal phenylketonuria. Am J Clin Nutr ; 67 : — 6.
Elevation of plasma tyrosine after a single oral dose of l -tyrosine. Life Sci ; 25 : — Phenylalanine and tyrosine kinetics in relation to altered protein and phenylalanine and tyrosine intakes in healthy young men. Am J Clin Nutr ; 56 : — Phenylalanine metabolism in humans: a reciprocal labeling study using [1- 13 C] and [3,3- 2 H 2 ] tracers. National Research Council. Recommended dietary allowances. Phenylalanine-tyrosine deficiency syndrome as a complication of the management of hereditary tyrosinemia.
Am J Clin Nutr ; 30 : — Twenty-four—hour l -[1- 13 C]tyrosine and l -[3,3- 2 H 2 ]phenylalanine oral tracer studies on generous, intermediate, and low phenylalanine intakes to estimate aromatic amino acid requirements in adults.
Am J Clin Nutr ; 67 : — Shiman R , Gray DW. Formation and fate of tyrosine. Intracellular partitioning of newly synthesized tyrosine in mammalian liver.
J Biol Chem ; : — 9. Diurnal variations in plasma concentrations of tryptophan, tyrosine, and other neutral amino acids: effect of dietary protein intake.
Am J Clin Nutr ; 32 : — Daily rhythms in the concentrations of various amino acids in human plasma. Plasma phenylalanine and tyrosine levels during the day in normal female controls and female obligate phenylketonuria heterozygotes. Enzyme ; 28 : — 7. Jakubovic A. Phenylalanine-hydroxylating system in the human fetus at different developmental ages. Biochim Biophys Acta ; : — Phenylalanine hydroxylase in human liver during development.
Pediatr Res ; 7 : 1 — 4. Lack of fetal effect on blood phenylalanine concentration in maternal phenylketonuria. J Pediatr ; : — 7. Low serum tyrosine in patients with phenylketonuria on dietary treatment. Lancet ; 1 : letter. Koepp P , Held KR. Serum tyrosine in patients with hyperphenylalaninaemia. Lancet ; 2 : 92 — 3. Plasma amino acids in phenylketonuric children treated either with phenylalanine-free amino acids or a protein hydrolysate.
Acta Paediatr Scand ; 79 : 69 — Fasting plasma amino acid concentrations in PKU children on two different levels of protein intake. Acta Paediatr Scand ; 77 : 60 — 6. Pediatrics ; 92 : — 3. Large daily fluctuations in tyrosine in treated patients with phenylketonuria PKU.
Am J Clin Nutr ; 64 : — Phenylketonuria PKU : the in-vivo hydroxylation rate of phenylalanine into tyrosine is decreased. J Clin Invest ; : — Nutrient intake and growth of infants with phenylketonuria undergoing treatment.
J Pediatr Gastroenterol Nutr ; 27 : — Bessman SP. J Pediatr ; 81 : — Diamond A. Acta Paediatr ; suppl : 89 — Lou H. Dopamine precursors and brain function in phenylalanine hydroxylase deficiency. Acta Paediatr ; suppl : 86 — 8. Welsh MC. A prefrontal dysfunction model of early-treated phenylketonuria.
Eur J Pediatr ; suppl : S87 — 9. Large neutral amino acids block phenylalanine transport into brain tissue in patients with phenylketonuria. Daily fluctuation of plasma amino acid levels in adult men: effect of dietary tryptophan intake and distribution of meals. J Nutr ; : 61 — Plasma amino acid response in young men given diets devoid of single essential amino acids. J Nutr ; : — Holme E , Lindstedt S.
J Inherit Metab Dis ; 21 : — 4. Berger R. Physician's guide to the laboratory diagnosis of metabolic diseases. Amino acids and proteins are the building blocks of life. When proteins are digested or broken down, amino acids are left. The human body uses amino acids to make proteins to help the body:.
Nonessential means that our bodies can produce the amino acid, even if we do not get it from the food we eat. Nonessential amino acids include: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine. You do not need to eat essential and nonessential amino acids at every meal, but getting a balance of them over the whole day is important. Lysine oxidation and F 13 CO 2 decreased linearly as Tyr intake increased, to a break point that was interpreted as the mean dietary Tyr requirement This represents
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