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1. The half-cystine content of ovotransferrin, measured as cysteic acid, was 31mol/80000g of protein. 2. The amino acid sequences of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin were studied. 3. 34 unique cysteic acid residues were identified. 4. It is concluded that hen ovotransferrin does not consist of two identical halves or subunits.
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1. The effects of the sulphur containing amino acids, homocysteic acid, homocysteine sulphinic acid, cysteic acid and cysteine sulphinic acid on the release of [3H]-acetylcholine ([3H]-ACh) from the cholinergic amacrine cells of the rabbit retina were examined. 2. All the compounds stimulated the spontaneous resting release and abolished the light-evoked release of [3H]-ACh. Except for homocysteine sulphinic acid these actions occurred at concentrations that did not affect the erg b-wave amplitude, indicating a site of action at the inner retina. 3. N-methyl-D-aspartate (in Mg(2+)-containing medium) clearly blocked the effects of homocysteic acid and homocysteine sulphinic acid on the resting release of [3H]-ACh but had no effect on the actions of cysteic acid and cysteine sulphinic acid. 4. Since N-methyl-D-aspartate is an antagonist of the light-evoked endogenous bipolar cell transmitter released onto cholinergic cells, these results are consistent with the suggestion that homocysteic acid or homocysteine sulphinic acid may be a transmitter released from this subpopulation of bipolar cells. 5. The present experiments indicate the existence of excitatory amino acids that have closer pharmacological properties to a bipolar cell transmitter than glutamate but it remains to be seen whether homocysteic acid or homocysteine sulphinic acid occur in these particular bipolar cells.
Concentrations of the sulfur-containing amino acids methionine, homocysteic acid, cysteic acid and taurine were measured in brain structures of young and old Wistar rats in an attempt to establish a possible link between the increase in oxidative stress with ageing and changes in tissue levels of these amino acids. Contrary to data reported by others, in all brain structures of young and old rats homocysteic acid levels could not be quantified. Compared with young rats, in old animals taurine and methionine concentrations significantly decreased in striatum and cortex; decreased taurine levels were also found in nucleus accumbens and cerebellum and lower concentrations of methionine were found in midbrain, hippocampus and pons-medulla. Cysteic acid levels either did not change or significantly increased in cortex and hippocampus. These results are discussed taking into account the biosynthesis of sulfur-containing amino acids in rat brain and the decrease in glutathione in relation to oxidative stress with ageing. Changes in aspartic acid, glutamic acid, serine, glutamine, glycine and GABA concentrations with ageing were also determined in the same brain structures and were in good agreement with those previously reported (Strolin Benedetti et al., 1990 a, b).
Cattle hair exposed to solutions of 35S-sulfide ions at pH 12.5, hydrolyzed with acid, and analyzed for amino acids with simultaneous measurement of the radioactivity of the eluate from the analytical column showed 87 percent of the radioactivity incorporated in the hair in three amino acids: cysteic acid, lanthionine, and cystine. This and other evidence presented lend further support to the intermediacy of dehydroalanyl residues formed by a beta-elimination reaction in the conversion of cystinyl residues to lanthionyl residues in proteins. The presence of radioactively labelled cystine in the hydrolyzate indicates that the dehydroalanyl residues are also capable of reforming cystinyl residues under these same conditions through a series of reversible reactions.
Cysteine sulfinic acid decarboxylase (EC 4.1.1.29) was purified from calf brain by pH precipitation, ammonium sulfate fractionation, gel filtration and DEAE-Sephadex A-50 chromatography. The enzyme preparation decarboxylated both cysteine sulfinic acid and cysteic acid at all steps of the purification and the ratio of the velocity of decarboxylation of cysteine sulfinic acid to that of cysteic acid was constant, about 2, throughout the purification procedure. The pH optimum was 7.2 both for cysteine sulfinic acid and cysteic acid. The molecular weight of the enzyme was estimated at 65 000 using gel filtration on a Sephadex G-200 column. Its Km's were 0.9 mM for cysteine sulfinic acid and 1.6 mM for cysteic acid, with Vmax values of 60.5 and 33.5 nmol/h(mg protein), respectively.
Endogenous synthesis of taurine by cats is limited. Putative precursors of taurine, cysteinesulfinic acid and cysteic acid, were fed to cats to determine whether they were utilized. Groups of five cats were depleted of taurine by a resin (Colestipol(R)) diet, then given 6 dietary treatments containing (g/kg diet): 0.0, 0.4, or 0.8 taurine; or 0.98 or 1.96 cysteinesulfinic acid, or 0.4 taurine + 1.0 cysteic acid for 12 wk. Plasma and whole blood taurine concentrations and body weights were measured weekly. Concentration of taurine in semitendinosus muscle was measured initially, after 2 wk of taurine depletion (after resin-diet), and monthly thereafter. The resin diet decreased concentrations of taurine in plasma, whole blood, and muscle to 0.20, 0.49, and 0.37 of initial values, respectively. Cysteinesulfinic acid diets resulted in no significant (P > 0.05) increase in the concentration of taurine in plasma, whole blood, or muscle, and no increased excretion of cysteinesulfinate or taurine in urine or feces. Cats fed the diets containing 1.0 g cysteic acid + 0.4 g taurine, or 0.8 g taurine/kg diet had similar concentrations of taurine in plasma, whole blood, and muscle. Aminotransferase activity for cysteinesulfinic acid in the liver and intestinal mucosa of cats and rats was higher than that for aspartic or cysteic acids. Transamination of dietary cysteinesulfinic acid to beta-sulfinylpyruvate (which spontaneously decomposes), rather than decarboxylation is postulated as the basis for no detectable conversion to taurine. In contrast, cysteic acid is reversibly transaminated to beta-sulfopyruvate which is stable and thereby is a precursor for taurine in cats.
In this paper, we present definitive data to show, from ESI (electrospray ionization) studies, that the thiol-bimane compound isolated and purified from Entamoeba histolytica trophozoites, corresponds unequivocally to the structure of trypanothione. Trypanothione disulphide was shown to have a molecular ion of m/z 722. It was further demonstrated by MALDI-TOF (matrix-assisted laser desorption ionization-time-of-flight) MS that this thiol compound also corresponds to the characteristic monoprotonated ion of trypanothione-(bimane)(2), which has a molecular ion of m/z 1103.95. The ion pattern of the thiol-bimane compound prepared from the commercial trypanothione standard is identical with the E. histolytica thiol-bimane compound. After HPLC separation, chemical amino acid analysis by dabsylation and dansylation of the thiol bimane compound from Entamoeba showed the presence of the following trypanothione components: glutamic acid, cysteic acid, glycine and spermidine. We can conclude from these highly reliable MS experiments and chemical analyses that E. histolytica contains the thiol compound trypanothione, which was previously thought to occur only in trypanosomatids.