Tryptophan riboflavin

Structures of ANS (l-anilinonaphthalene-8-sulfonate), L-tryptophan, riboflavin or flavin, ethidium bromide (EB), TNS, and NADH. 

The first step in XJVR-induced skin cancer is UVR-initiated DNA mutation, which causes the transformation of the normal cells to malignant cells. For UVR to initiate a biological reaction, it has to be absorbed by endogenous molecules (chromophores). UVB is absorbed directly by the DNA, and therefore can directly induce DNA mutation (224), in the form of thymine dimer formation (289). Some protein components may also ad as chromophores for UVB (224). UVA is absorbed by the reduced forms of the co-enzymes nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide phosphate (NADPH), tryptophan, riboflavin, and melanin (224,290). UVA-induced DNA damage is believed to be mediated by oxygen reactive species that are released after the absorption of UVA by those endogenous chromophores and results in photooxidation of selected bases... 

The level of these potential carcinogens in some broiled or roasted foods, such as broiled sardines, is about 10 ng/g. This amount is much lower than those used in the carcinogenicity assays. The long-term cumulative effect of the carboline intake may be of great concern. In some experimental studies, tryptophan itself appears to promote the formation of tumors.287-289 Also, a tryptophan-riboflavin photoinduced adduct may have a role in the pathogenesis of hepatic dysfunction observed during parenteral nutrition.290... 

Donoso, M. L. N., Valenzuela, A., and Silva, E., Tryptophan-riboflavin photo-induced adduct and hepatic dysfunction in rats, Nutr. Rep. Int., 37, 599, 1988. 

Kulinski, T., Visser, A. J. W. G., O Kane, D. J., and Lee, J. (1987). Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi. Biochemistry 26 540-549. 

Glutaric acidurias Type I Primary defect of glutarate oxidation Type II Defect of electron transfer flavoprotein Type I Severe basal ganglia/cerebellar disease with macrocephaly. Onset 1-2 years Type II Fulminant neurological syndrome of the neonate. Often with renal/hepatic cysts. Usually fatal Diet low in lysine and tryptophan Supplementation with coenzyme Q, riboflavin, carnitine... 

Riboflavin (vitamin Bj) is chemically specified as a 7,8-dimethyl-10-(T-D-ribityl) isoalloxazine (Eignre 19.22). It is a precnrsor of certain essential coenzymes, such as flavin mononucleotide (FMN) and flavin-adenine dinucleotide (FAD) in these forms vitamin Bj is involved in redox reactions, such as hydroxylations, oxidative carboxylations, dioxygenations, and the reduction of oxygen to hydrogen peroxide. It is also involved in the biosynthesis of niacin-containing coenzymes from tryptophan. 

The most obvious fluorescent compound in milk is riboflavin, which absorbs strongly at 440-500 nm and emits fluorescent radiation with a maximum at 530 nm. Riboflavin in whey is measured easily by fluorescence (Amer. Assoc. Vitamin Chemists 1951). Proteins also fluoresce because of their content of aromatic amino acids. Part of the ultraviolet radiation absorbed at 280 nm is emitted at longer wavelengths as fluorescent radiation. A prominent maximum near 340 nm is attributable to tryptophan residues in the protein. Use of fluorescence for quantitation of milk proteins was proposed by Konev and Kozunin (1961), and the technique has been modified and evaluated by several groups (Bakalor 1965 Fox et al. 1963 Koops and Wijnand 1961 Porter 1965). It seems to be somewhat less accurate than desired because of difficulties in disaggregating the caseinate particles and in standardizing instruments. It also involves a basic uncertainty due to natural variations in the proportions of individual proteins which differ in tryptophan content. 

For a highly fluorescent molecule such as riboflavin, < )f may be 0.25 or more.129 For tryptophan in water it is about 0.14, and in proteins it varies from near zero to 0.35.130... 

Yeast protein is easily digested (87%) and provides amino acids essential to human nutrition. Most commercial yeasts show the following pattern of amino acids, among others, as percent of protein 8.2% lysine 5.5% valine 7.9% leucine 2.5% methionine 4.5% phenylalanine 1.2% tryptophan 1.6% cystine 4% histidine 5% tyrosine and 5% arginine. The usual therapeutic dose of dried yeast is 40 grams/day, which supplies significant daily needs of thiamine, riboflavin, niacin, pyridoxine, and general protein. 

Since ANS dissolved in a polar medium does not fluoresce, one cannot record its fluorescence excitation spectrum. For tryptophan, ethidium bromide, and riboflavin, one can see that for each molecule, the absorption spectrum looks like the fluorescence... 

Niacin and riboflavin are converted to their respective coenzymes, NAD+ and NADP+ on the one hand and flavin munonucleotide (FMN) and flavin adenine dinucleotide (FAD) on the other, as described in Chapter 10. Some NAD+ can be synthesized from tryptophan, as described in Chapter 20. Tryptophan, however, provides only a fraction of our daily NAD+ requirements. 

The disturbance of tryptophan metabolism in riboflavin deficiency, caused by impairment of kynurenine hydroxylase, can also result in reduced synthesis of NAD from tryptophan. This may therefore be a factor in the etiology of pellagra (Section 8.3.3.1). 

Kynurenine Hydroxylase Kynurenine hydroxylase is an FAD-dependent mixed-function oxidase of the outer mitochondrial membrane, which uses NADPH as the reductant. The activity of kynurenine hydroxylase in the liver of riboflavin-deficient rats is only 30% to 50% of that in control animals, and deficient rats excrete abnormally large amounts of kynurenic and anthranilic acids after the administration of a loading dose of tryptophan, and, correspondingly lower amounts of quinolinate and niacin metabolites. Riboflavin deficiency may thus be a contributory factor in the etiology of pellagra when intakes of tryptophan and niacin are marginal (Section 8.5.1). 

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