Alanine- 3-sulfonic acid

Aromatic Sulfonic Acids as Reagents for Amino Acids. The Preparation of 1-Serine, 1-Alanine, 1-Phenylalanine, and 1-Leucine from Protein Hydrolysates J. biol. Chem. 143, 121 (1942). 

Calcium dihydroxide. See Calcium hydroxide Calcium d(+)-N-(a,y-dihydroxy-p,p-dimethylbutyryl)-p-alaninate Calcium N-(2,4-dihydroxy-3,3-dimethyl-1-oxobutyl-P-alanine. See Calcium D-pantothenate Calcium diiodide. See Calcium iodide Calcium dilactate. See Calcium lactate Calcium dinitrate. See Calcium nitrate Calcium dinonyinaphthalene sulfonate CAS 57855-77-3 68425-34-3 Synonyms Dinonyinaphthalene sulfonic acid, calcium salt Naphthalenesulfonic acid, dinonyl-, calcium salt Empirical C28H44O3S V2Ca Properties M.w. 480.80 Uses Rust/corrosion inhibitor demulsifier in oils grease penetrant... 

Branched and hindered aldehydes have been enantioselectively Q -aminated in high yield in THF solution at 0°C with azodicarboxylates, using a simple amino acid catalyst such as 3-(l-naphthyl)alanine, as its hydrochloride." An ion-pair catalyst formed by mixing a cinchona-derived diamine and camphor-sulfonic acid gives high yield and ee in direct amination of a-branched aldehydes, using azodicarboxylates." ... 

All of the above features make silica colloidal crystals ideal candidates for highly selective responsive nanoporous membranes. However, until 2005, there were no publications describing transport through surface-modified colloidal membranes. In 2005, Zharov group introduced, for the first time, the concept of permselective colloidal nanoporous membranes by describing pH-responsive amine-modified colloidal membranes with controlled transport of positively charged species [26]. Later, they reported a detailed study of transport through amine-modified colloidal membranes [27], as well as membranes modified with sulfonic acids [28,29], Methods to modify the colloidal nanopores with polymers were developed [30], which allowed us to introduce temperature-responsive poly(A-isopropylacrylamide) (PNIPAAM) [31], pH- and ion-responsive poly(2-(dimethylamino)ethyl methacrylate), PDMAEMA [32], and pH- and temperature-responsive poly(L-alanine) [33], and to study the molecular transport in these polymer-modified nanoporous coUoidal membranes as a function of the environmental conditions. In this chapter we summarize these results. 

A satisfactory isolation procedure has been described recently by Stdn et al. (755). After refiuxing silk fibroin for 8 hours with concentrated hydrochloric acid, the bulk of the acid is removed by vacuum distillation and treatment with lead acetate. Tyrosine is removed, the concentrated filtrate is treated with a solution of 5-nitronaphthalene-l-sulfonic acid dihydrate and the slightly soluble glycine naphthalene sulfonate is removed. Methyl cellosolve and a solution of azobenzene-p-sulfonic acid trihydrate are added, the suspension is filtered and the precipitate of L-alanine azobenzene sulfonate is treated with barium acetate. The suspension of barium azobenzene sulfonate is filtered and the L-alanine obtained from the filtrate is recrystallized from aqueous ethanol see p. 359. 

Tetrahydroharmine (see Volume VIII, p. 47) has been obtained from natural sources in the (4- )-form. The racemic base was resolved by means of camphor-7T-sulfonic acid and the formyl derivative of the (-)-form degraded by ozone oxidation to V-carboxyethyl-L-alanine. The natural base therefore has the R configuration (LXXXIII R = OMe) (227) and belongs to the same stereochemical series as (-f )-l,2,3,4-tetrahydroharman (LXXXIII R = H) (228). 

The influence of an exchange of the phenyl group for a methyl resp. benzyl group was studied with polymer 7 resp. 8. These OAP were obtained from polystyrenesulfochloride and L-alanine resp. L-phenylalanine. The coupling reaction was performed in a dioxane/ water mixture with a threefold excess of the amino acid in the presence of triethylamine. The yield i.e. the exchange of the active chlorine of the polystyrenesulfochloride with the amino acid residue was 49% (6), 61% (7), resp. 62% (8). The unreacted chlorosulfonyl groups were transformed to sulfonic acid groups [7, 8]. 

Clear separation of the clupeine Y fraction into two components, YI and YII, is now desired. 2,4,6-Trinitrobenzene sulfonic acid (TNBS) is known to selectively modify amino groups in a peptide chain to yield trinitrophenyl (TNP) derivatives but never to react with imino groups (Okuyama and Satake, 1960). Thus, the N-terminal alanine residue of clupeine YI and Z should be trinitrophenylated while the N-terminal proline of clupeine YII is not, so that modification of whole clupeine with TNBS will give TNP-clupeine YI, TNP-clupeine Z and free clupeine YII. Some differences are then expected in the power of a resin to adsorb free and trinitrophenylated protamine components. 

Auxiliary Synthesis Both the (S)- and (R)- enantiomers of the camphor-derived ACC 54 are available in seven steps from commercially available and inexpensive (S)- and (R)-camphor sulfonic acid, respectively (Scheme 7.9). The seven-step process provides an overall yield of approximately 40%. A key step in the synthesis of 54 and 55 is the direct A -amination of the corresponding oxazolidinones, 61 and 62. This transformation is effectively achieved in a straightforward manner using a modification of a procedure recently reported by Hynes et al. ° Application of this amination procedure to commercially available (R)- or (5)-4-benzyloxazolidinone ((R)-62 or (S)-62, respectively) provides phenyl alanine-derived auxiliaries (R)-55 or (S)-55 in excellent yield. 

Oligomers of glycine show little appreciable retention on octyl silica with 20 mM phosphate buffers over the pH range 2.10-7.83 (46), or on octadecyl silica with 100 mM phosphate buffer, pH 2.1 (33), or 5 mM phosphate buffers, pH 2.1, containing hydrophobic alkyl sulfonates (30). It is thus likely that the peptide chain proper makes only a very small contribution to the retention of peptides under these conditions. Based on partition coefficient considerations, oligomers of alanine, and the other nonpolar amino acids, should show a linear dependence of log A on the number of residues. This, in fact, has been observed. For example, the plot of log A versus the number of alanine residues shows (33) a linear dependence with a uniform log A increment due to the methyl group of the aliphatic side chain (Fig. 2), i.e., the effect is additive (45a, 46a). 

Following oral administration 7-22% of alitame is unabsorbed and excreted in the feces. The remaining amount is hydrolyzed to aspartic acid and alanine amide. The aspartic acid is metabolized normally and the alanine amide excreted in the urine as a sulfoxide isomer, as the sulfone, or conjugated with glucuronic acid. 

M22. Munier, R. L., and Sarrazin, G., Chromato-electrophorese des amino acides en couche mince de poudre de cellulose. I. Cas des amino acides de faible mobilite alanine, asparagine, glutamine, glycocolle, methionine sulfone, mdthionine sulf-oxyde, proline, sdrine and threonine. Bull. Soc. Chim. Fr. pp. 1363-1365 (1966). 

Figure 3.16 Determination of amino acid composition. Different amino acids in a peptide hydrolysate can be separated by ion-exchange chromatography on a sulfonated polystyrene resin (such as Dowex-SO). Buffers (in this case, sodium citrate) of increasing pH are used to elute the amino acids from the column. The amount of each amino acid present is determined from ihe absorbance. Aspartate, which has an acidic side chain, is first to emerge, whereas arginine, which has a basic side chain, is the last. The original peptide is revealed to be composed of one aspartate, one alanine, one phenylalanine, one arginine, and two glycine residues.

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