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Amino sulfur containing

Since dietary cereals are low in sulfur-containing amino acids, they produce an alkaline urine which favors the retention of bone minerals. In post-menopausal women, there appears to be some interaction between the diet and the effect produced by estrogens on bone mineral content (28). [Pg.352]

Sulfur deficiency usually is not a problem for mminants because the mminal microflora can utilize sulfur-containing amino acids. A deficiency can occur, however, when an NPN source is fed. L-Methionine [63-68-3] is the most biologically available source of sulfur (21). Various sulfates are intermediate in sulfur avadabiHty, and elemental sulfur is the least available source of sulfur. [Pg.156]

Gelatin can be a source of essential amino acids when used as a diet supplement and therapeutic agent. As such, it has been widely used in muscular disorders, peptic ulcers, and infant feeding, and to spur nail growth. Gelatin is not a complete protein for mammalian nutrition, however, since it is lacking in the essential amino acid tryptophan [73-22-3] and is deficient in sulfur-containing amino acids. [Pg.208]

The differences in the amino acid chemistry of the hide coUagen and the hair keratin are the basis of the lime-sulfide unhairing system. Hair contains the amino acid cystine. This sulfur-containing amino acid cross-links the polypeptide chains of mature hair proteins. In modem production of bovine leathers the quantity of sulfide, as Na2S or NaSH, is normally 2—4% based on the weight of the hides. The lime is essentially an unhmited supply of alkah buffered to pH 12—12.5. The sulfide breaks the polypeptide S—S cross-links by reduction. Unhairing without sulfide may take several days or weeks. The keratin can be easily hydrolyzed once there is a breakdown in the hair fiber stmcture and the hair can be removed mechanically. The coUagen hydrolysis is not affected by the presence of the sulfides (1—4,7). [Pg.83]

Calculated as sulfur-containing amino acids, methionine plus cystine. Serving corresponds to 236 mL (1 cup) unless otherwise noted. Serving corresponds to 113 g (4 oz). [Pg.378]

Fig. 1. The side chain R of the 20 standard amino acids +H3N—CHR—COO at pH 7. For proline, the complete stmcture is shown. Amino acid side chains can be categorized as aUphatic (Gly, Ala, Val, Leu, and He), hydrophilic (Ser, Thr, Asp, Glu, Asn, Gin, Lys, and Arg), sulfur-containing (Cys and... Fig. 1. The side chain R of the 20 standard amino acids +H3N—CHR—COO at pH 7. For proline, the complete stmcture is shown. Amino acid side chains can be categorized as aUphatic (Gly, Ala, Val, Leu, and He), hydrophilic (Ser, Thr, Asp, Glu, Asn, Gin, Lys, and Arg), sulfur-containing (Cys and...
Sulfoxides occur widely in small concentrations in plant and animal tissues, eg, aHyl vinyl sulfoxide [81898-53-5] in garlic oil and 2,2 -sulfinylbisethanol [3085-45-8] as fatty esters in the adrenal cortex (1,2). Homologous methyl sulfinyl alkyl isothiocyanates, which are represented by the formula CH3SO(CH2) NCS, where n = 3 [37791-20-1], 4 [4478-93-7], 5 [646-23-1], 8 [75272-81-0], 9 [39036-83-4], or 10 [39036-84-5], have been isolated from a number of mustard oils in which they occur as glucosides (3). Two methylsulfinyl amino acids have also been reported methionine sulfoxide [454-41-1] from cockroaches and the sulfoxide of i -methylcysteine, 3-(methylsulfinyl)alaiiine [4740-94-7]. The latter is the dominant sulfur-containing amino acid in turnips and may account in part for their characteristic odor (4). [Pg.107]

The side groups of the amino acids vary markedly in size and chemical nature and play an important role in the chemical reactions of the fiber. For example, the basic groups (hisidine, arginine, and lysine) can attract acid (anionic) dyes, and in addition the side chains of lysine and hisidine are important sites for the attachment of reactive dyes. The sulfur-containing amino acid cysteine plays a very important role, because almost all of the cysteine residues in the fiber are linked in pairs to form cystine residues, which provide a disulfide bridge —S—S— between different polypeptide molecules or between segments of the same molecules as shown ... [Pg.343]

Potential consumer benefits from biotechnology (56) are cost and quaUty. The use of biotech means to increase the level of various sulfur-containing amino acids in coffee proteins, and to enhance sucrose and oil levels, could have an impact on the flavor and aroma of the finished ground coffee product. Also, caffeine level modification/elimination through genetic manipulations of the coffee plant could yield low caffeine coffee without additional processing by the manufacturer. [Pg.390]

The Dim ester was developed for the protection of the carboxyl function during peptide synthesis. It is prepared by transesterification of amino acid methyl esters with 2-(hydroxymethyl)-l,3-dithiane and Al(/-PrO)3 (reflux, 4 h, 75°, 12 torr, 75% yield). It is removed by oxidation [H2O2, (NH4)2Mo04 pH 8, H2O, 60 min, 83% yield]. Since it must be removed by oxidation it is not compatible with.sulfur-containing amino acids such as cysteine and methionine. Its suitability for other, easily oxidized amino acids (e.g., tyrosine and tryptophan) must also be questioned. It is stable to CF3CO2H and HCl/ether. - ... [Pg.243]

The nonpolar amino acids (Figure 4.3a) include all those with alkyl chain R groups (alanine, valine, leucine, and isoleucine), as well as proline (with its unusual cyclic structure), methionine (one of the two sulfur-containing amino acids), and two aromatic amino acids, phenylalanine and tryptophan. Tryptophan is sometimes considered a borderline member of this group because it can interact favorably with water via the N-H moiety of the indole ring. Proline, strictly speaking, is not an amino acid but rather an a-imino acid. [Pg.83]

Mammalian sulfite oxidase is the last enzyme in the pathway for degradation of sulfur-containing amino acids. Sulfite oxidase (SO) catalyzes the oxidation of sulfite (SO ) to sulfate (S04 ), using the heme-containing protein, cytochrome c, as electron acceptor ... [Pg.441]

On treatment of 5-amino-l,2,3,4-thiatriazole with concentrated hydrochloric acid Freund and Schander obtained a hydrochloride of a sulfur-containing substance which was thought to be a three-membered ring compound [cf. Eq. (19)]. The possibility that it might be a dimer with a six-membered ring was, however, left open. [Pg.281]

Thiols, thioethers and sulfoxides [37-39] e.g. sulfur-containing amino acids... [Pg.187]

The R groups of amino acids determine their unique biochemical functions. Amino acids are classified as basic, acidic, aromatic, aliphatic, or sulfur-containing based on the properties of their R groups. [Pg.20]

Cooper AJL Biochemistry of the sulfur-containing amino acids. Annu RevBiochem 1983 52 187. [Pg.262]

Forman, H.J., Rotman, E.I. and Fisher, A.B. (1983). Roles of selenium and sulfur-containing amino acids in protection against oxygen toxicity. Lab. Invest. 49, 148-153. [Pg.258]

Scheme 3.30 Sulfur-containing p-amino alcohol ligands for addition of ZnEt2 to benzaldehyde. Scheme 3.30 Sulfur-containing p-amino alcohol ligands for addition of ZnEt2 to benzaldehyde.

See other pages where Amino sulfur containing is mentioned: [Pg.476]    [Pg.379]    [Pg.271]    [Pg.493]    [Pg.490]    [Pg.68]    [Pg.393]    [Pg.4]    [Pg.182]    [Pg.248]    [Pg.1069]    [Pg.663]    [Pg.252]    [Pg.159]    [Pg.1081]    [Pg.344]    [Pg.50]    [Pg.85]    [Pg.291]    [Pg.337]    [Pg.272]    [Pg.1081]    [Pg.28]    [Pg.88]    [Pg.105]    [Pg.120]    [Pg.123]    [Pg.141]    [Pg.144]   
See also in sourсe #XX -- [ Pg.84 ]

See also in sourсe #XX -- [ Pg.84 , Pg.301 , Pg.358 ]




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Amino acid sulfur-containing oxidation

Catabolism sulfur-containing amino acids

Hydroxyl radical sulfur-containing amino acids

Sulfur amino acids residues containing

Sulfur-containing

Sulfur-containing amino acid, absence

Sulfur-containing amino acids

Sulfur-containing amino acids, and

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