The photodecomposition of tryptophan peptides

Aqueous solutions of the four trytophan peptides, Ala-Trp-Val, Val-Trp-Ala, Ala-Ala-Trp-Val and Ala-Gly-Trp-Leu, have been irradiated with light of wavelengths >295 n. The major changes were destruction of the tryptophan residue, liberation of ammonia and the formation of photoproducts of increased molecular weight. Up to 40% of Ala-Ala-Trp-Val and Ala-Gly-Trp-Leu were converted to products with molecular weights ranging from two to four times those of the original tetrapeptides. Most of the yellow material formed during irradiation in air was present in the high molecular weight fractions. Irradiation of Ala-Gly-[¹⁴C]Trp-Leu gave the following identifiable photoproducts: Ala-Gly-Asp-Leu, Ala-Gly-(N′-formyl)Kyn-Leu, Ala-Gly-Oia-Leu, and ammonia, where Kyn means kynurenine and Oia, β-(3-oxidolyl)alanine.     

The hydroxylation of tryptophan.

Products of the chemical hydroxylation of tryptophan by Fenton and Udenfriend reactions are similar to those obtained by ionizing radiation. When tryptophan is exposed to either of these systems, a mixture of four hydroxytryptophans, oxindole-3-alanine, and N-formylkynurenine is formed. This observation indicates that the hydroxyl radical attacks the aromatic nucleus as well as the 2 and 3 positions of the pyrrole ring. During gamma-radiolysis of nitrous oxide-saturated tryptophan solution and in the absence of oxygen or ferric edta, the hydroxyl radical adduct (or hydroxycyclohexadienyl radical) of tryptophan undergoes dimerization and polymerization, which results in a yellow product with maximal absorbance at 425 nm. In the presence of ferric edta, or in a Fenton system, the hydroxyl radical adduct disproportionates, and hydroxylated derivatives are formed. The yields of the hydroxytryptophans are proportional to the concentration of ferric edta to a limiting yield of 54% of the theoretical yield, which is taken to be one hydroxylated product per two hydroxyl radicals. Under these conditions, 4-, 5-, 6-, and 7-hydroxy-derivatives of tryptophan are found in the proportion 4:2:2:3, respectively. The presence of dioxygen during gamma-radiolysis increases the yield of N-formylkynurenine, but does not affect the total yield of hydroxytryptophans. Similarly, tryptophan subjected to the Udenfriend reaction yields 4-, 5-, 6-, and 7-hydroxytryptophan and N-formylkynurenine in approximately equal amounts.     

分光光度法测定豆类及其粗蛋白质中的色氨酸

建立一种快速、准确测定各种豆类试样及粗蛋白质中的色氨酸含量的分光光度法讨论最佳试验条件及试剂用量,反应物在410nm处具有最大吸收波长ε=1.103×104L·mol-1·cm-1,回收率93.50-110.20%,相对标准偏差RSD＜2.61.     

Tryptophan catabolism by tryptophan pyrrolase in rat liver. The effect of tryptophan loads and changes in tryptophan pyrrolase activity.

We investigated how changes in tryptophan pyrrolase activity and tryptophan loads affect the breakdown of tryptophan was estimated by injecting rats with [ring-2-14-C]tryptophan and measuring respiratory 14-CO2. We concluded, contrary to previous reports, that induction of tryptophan pyrrolase definitely will increase the rate of tryptophan breakdown. Tryptophan loads also increase tryptophan breakdown even in circumstances where there is no increase in tryptophan pyrrolase activity, presumably by increasing the saturation of the enzyme. After a tryptophan load (50 mg per kg) the increase in liver tryptophan concentration lasts only 30 min. The rapid return of liver tryptophan to normal may be due partly to the high turnover rate of liver tryptophan. We estimate that tryptophan pyrrolase degrades tryptophan in vivo at a rate that is equivalent to the whole liver tryptophan concentration in 7.5 min or less.     

The significance of tryptophan in human nutrition

Summary Aside from its role as one of the limiting essential amino acids in protein metabolism, tryptophan (TRP) serves as precursor for the synthesis of the neurotransmitters serotonin and tryptamine as well as for the synthesis of the antipellagra vitamin nicotinic acid and the epiphyseal hormone melatonin.By involvement in so manifold pathways, TRP and its metabolites regulate neurobehavioral effects such as appetite, sleeping-waking-rhythm and pain perception. TRP is the only amino acid which binds to serum albumin to a high degree. Its transport through cell membranes is competetrvely inhibited by large neutral amino acids (NAA). The TRP/NAA ratio in plasma is essential for the TRP availability and thus for the serotonin synthesis in the brain.Due to its high TRP-concentration, human milk protein provides optimal conditions for the availability of the neurotransmitter serotonin. Low protein cow's milk-based infant formulas supplemented with-lactalbumin — a whey protein fraction containing 5.8% TRP — present themselves as a new generation of formulas, with an amino acid pattern different from the currently used protein mixtures of adapted formulas, resembling that of human milk to a much higher degree.