Column chromatography of cysteinesulfinic acid, cysteic acid, and s-sulfocysteine.
Explore the source record for details and available documents.
Amino Acids↗
SEARCH · PubMed Health
Results for “Cysteic Acid”
Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
Tissue and regional distribution of cysteic acid decarboxylase. A new assay method.
A sensitive and rapid assay method method for cysteic acid decarboxylase was develped which combined the selectivity of ion exchange resin (a complete retention of the substrate, cysteic acid, and exclusion of the product, taurine) with the speed of a vacuum filtration. The synthesis and purification of 35S-labeled cysteic acid were described. The validity of the assay was established by the identification of the reaction product as taurine. With this new method, the decarboxylase activity was measured in discrete regions of bovine brain. Putamen had the highest activity, 172 pmol taurine formed/min/mg protein (100%), followed by caudate nucleus, 90%; cerebral cortex, 82%; hypothalamus, 81%; cerebellar cortex, 79%; cerebellar peduncle, 59%; thalamus, 42%; brain stem, 25%; pons, 10%; and corpus callosum, 3%. The decarboxylase activity in various mouse tissues was also determined as follows: liver, 403; brain, 145; kidney, 143; spinal cord, 59; lung, 21; and spleen, 10 pmol taurine formed/min/mg. No activity could be detected in skeleton muscle and heart, suggesting a different biosynthetic pathway for taurine synthesis in these tissues. The advantages and disadvantages of the new assay method are also discussed.
Animals↗
Utilization of L-methionine sulfoxide, L-methionine sulfone and cysteic acid by the weanling rat.
Three experiments were conducted to test the ability of weanling rats to utilize the oxidized forms of the sulfur amino acids methionine and cysteine for growth. In the first two experiments, diets were fed which contained graded levels of methionine, methionine sulfoxide and methionine sulfone. The third experiment included a comparison of two dietary levels of cysteine and cysteic acid. The 2 week weight gain and food consumption data indicated that methionine sulfoxide was utilized for growth with only 60% of the efficiency of that achieved by rats fed methionine. Methionine sulfone was not utilized for growth. Analysis of plasma sulfur amino acids showed that the rat has a limited capacity to utilize methionine sulfoxide by effecting its reduction to methionine. Cysteic acid did not support weight gain. This amino acid appeared to be rapidly catabolized to taurine. It was concluded that methionine sulfone and cysteic acid cannot be utilized by the weanling rat. Methionine sulfoxide cannot fully meet the dietary requirement of the rat methionine because of its limited capacity to reduce this amino acid.
Amino Acids↗
A sensitive radiometric assay for cysteic acid decarboxylase activity in crude enzyme preparations of rat liver and brain.
1. A method is described for the synthesis of L-[U-14C]cysteic acid from L-[U-14C] cysteine hydrochloride and for its subsequent utilisation as a substrate for cysteic acid decarboxylase activity in liver and brain. 2. The enzyme determination relies on the entrapment of radio-labelled carbon dioxide in Hyamine hydroxide. 3. The assay is sensitive, reliable and convenient and is particularly suitable for measuring the activity of the decarboxylase in crude enzyme preparations.
Animals↗
Keratin decomposition by dermatophytes. II. Presence of s-sulfocysteine and cysteic acid in soluble decomposition products.
The dermatophyte Microsporum gypseum was grown on human hair in a mineral medium. Filtrates of cultures of various age were chromatographed on Sephadex gels and further characterized by chemical analysis and thin-layer chromatography. The products of keratin decomposition were separated into two fractions. The first fraction formed 10 to 20% of the bulk and contained proteins low in sulfur content. The second, very wide fraction contained oligopeptides and polypeptides with molecular weights from several hundreds up to approximately 13,000 with a peak at 1,000-2,000 daltons. This fraction contained a relatively high amount of cystine, S-sulfocysteine, and cysteic acid. S-sulfocysteine was present in the free state and also combined in peptides where its amount exceeded that of cystine. This supports the author's hypothesis on keratin decomposition by dermatophytes. According to this hypothesis, the fungus excretes sulfite which cleaves the disulfide bonds of keratin to cysteine and S-sulfocysteine. The substrate, denatured by sulfitolysis, is then more easily digestible by fungal proteases. Besides S-sulfocysteine, comparable amounts of cysteic acid were found in all analyses. This compound most probably originated by air oxidation of sulfur amino acids in the alkaline cultivation fluid.
Biodegradation, Environmental↗
[Existence of cysteic acid and taurine in sporulating cells of Bacillus subtilis NRRL B558 (author's transl)].
Explore the source record for details and available documents.
Amino Acids, Sulfur↗
35S-Sulfide incorporation during alkaline treatment of keratin and its relation to lanthionine formation.
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.
Alanine↗
Oxidation of L-cystine by dimethyl sulfoxide. Cysteic acid-sulfoxide compounds.
Explore the source record for details and available documents.
Amino Acids, Sulfur↗
Taurine, analogues and ethanol elicited responses.
The effect of taurine, of some of its precursors and major metabolic products on spontaneous locomotor activity were studied in mice. The effect of taurine and some analogues on certain ethanol-mediated responses were observed. Administration of taurine, 50 mg/kg, IP, did not significantly alter motility in experimental animals compared to controls. Behavioral depression was evident subsequent to injection of cysteine hydrochloride or taurocholic acid (50 mg/kg). Administration of taurocholic acid, 50 mg/kg, IP, 30 min prior to a narcotic dose of ethanol, 5 g/kg, IP, reduced the time required for the onset of ethanol-narcosis. Pretreatment with cysteic acid, 50 mg/kg, IP, prolonged ethanol-produced narcosis. Treatment with cysteic acid 30 min prior to ethanol, 2.5 g/kg, IP, was found to decrease whole blood ethanol concentration as compared to the respective controls without a concomitant changes in brain ethanol levels. Administration of taurocholic acid, 100 mg/kg, IP, decreased the intake of an ethanol solution in rats preferring 5% ethanol solution over water as the drinking fluid of choice. None of the compounds tested altered endogenous specific activity of mouse liver alcohol dehydrogenase when given once daily (50 mg/kg, IP) for 10 consecutive days. The results suggest that both taurocholic acid and cysteic acid exert additive action to some ethanol-elicited responses studied.
Alcohol Drinking↗
Purification and characterization of mitochondrial cysteine aminotransferase from rat liver.
Cysteine aminotransferase has been purified over 300-fold from rat liver mitochondria. Transamination between L-cysteine and 2-oxoglutarate, and the reverse reaction, were observed to be catalyzed by the purified enzyme but inhibited by L-aspartate. The enzyme also catalyzed transamination of alanine, 3-sulfinic acid, aspartic acid, and cysteic acid. A new reaction assay method was devised, contributing an indication that mitochondrial cysteine aminotransferase is identical to mitochondrial aspartate aminotransferase. The latter apparently catalyzed 3 transamination reactions in the cysteine degradation process within mitochondria.
Animals↗
Amino acids in the synaptic vesicle fraction from calf brain: content, uptake and metabolism.
A synaptic vesicle fraction was prepared from calf brain cortex, containing 10 identified amino acids and two unidentified ninhydrin-positive compounds, one of which is apparently a peptide. The most plentiful amino acids were taurine (1.8 nmol/g original tissue), glutamic acid (1.8), serine (0.9), aspartic acid (0.8) and GABA (0.8); the others identified were cysteic acid (or cysteinesulphinic acid), glutamine, alanine, glycine and lysine. The unknown peptide occurred in a high concentration (about 16 alanine equivalents/g), and contained mainly aspartic acid and serine. Cysteic acid (or cysteinesulphinic acid) also occurred in relatively high amounts, but its peak contained acid-labile impurities. The influx of [14C]glutamate into the vesicles took place by means of non-saturable migration, while two saturable systems having very similar properties were dominant only at low glutamate concentrations. Influx constants for these quantitatively low uptake systems were Km, 34 and 92 micrometer, and Vmax, 33 and 49 nmol/min/g obtained by v versus v/S plot. Almost the same values were also obtained by a 1/v versus 1/S plot. GAD and GABA-T activities in the vesicles were only 1/200th of those in the synaptosomes.
4-Aminobutyrate Transaminase↗
Soluble and membrane-bound aspartate-binding activities in Salmonella typhimurium.
The specificities of the soluble and membrane aspartate-binding activities were compared with each other and with the specificity of aspartate chemotaxis and were found to be distinct. The soluble aspartate-binding protein was purified to homogeneity and had a molecular weight of 30,000. The dissociation constant was 10(-6) M for aspartate, and the protein bound glutamate, cysteic acid, and 2-amino-3-phosphonopropionate. Aspartate transport was inhibited by cysteic acid.
Aspartic Acid↗
Effect of ultra-high-temperature steam injection processing on sulfur-containing amino acids in milk.
Raw skim milk was processed by a modified No-Bac Unitherm IV System (Cherry-Burrell Corp.) at 143 C for 8 s, vacuum cooled to 71 C, collected, and cooled to 4 C. Raw and ultra-high-temperature processed skim milks were oxidized with performic acid, hydrolyzed with hydrochloric acid, and analyzed for cysteine and cystine (as cysteic acid) and methionine (as methionine sulfone) on a Beckman Automatic Amino Acid Analyzer. A loss of approximately 34% of these amino acids was observed in ultra-high-temperature processed skim milk. Sulfhydryl and disulfide groups determined with Ellman's reagent [5,5'-dithiobis(2-nitrobenzoic acid)] indicated no free sulfhydryls in raw skim milk and .07 mmole per liter in ultra-high-temperature processed skim milk. Loss in total sulfhydryl and disulfide groups was approximately 16% in ultra-high-temperature processed milk. Volatile sulfur compounds were detected by odor in the vapor collected from the vacuum chamber, but they could not be identified. Amino acid analysis of milk deposit collected from the injection section revealed .09 microgram of cysteine and cystine (as cysteic acid) per gram of deposit and no detectable methionine.
Amino Acids, Sulfur↗
Derivatization of cysteine and cystine for fluorescence amino acid analysis with the o-phthaldialdehyde/2-mercaptoethanol reagent.
Previous reports (Drescher, D.G., and Lee, K.S. (1978) Anal. Biochem. 84, 559-569; Lee, K.S., and Drescher, D.G. (1978) Int. J. Biochem. 9, 457-467) have shown that high performance liquid chromatographic analysis of amino acids with the o-phthaldialdehyde/2-mercaptoethanol reagent (OPA/2-ME) is one of the most sensitive procedures currently available for micro amino acid analysis. In the present paper, methods are presented for the modification of cysteine and cystine in proteins for micro amino acid analysis using OPA/2-ME. Cysteine and cystine, which both show low fluorescence with OPA/2-ME, are converted to cysteic acid with performic acid directly, or to S-3-sulfopropylcysteine with 1,3-propane sultone after reduction of cystine with tri-n-butylphosphine. Cysteic acid and S-3-sulfopropylcysteine form highly fluorescent adducts with OPA/2-ME. The formation of S-3-sulfopropylcysteine in proteins and the subsequent hydrolysis of the proteins with methanesulfonic acid are particularly useful for complete amino acid analysis at the picomole level using a single sample.
Aldehydes↗
[Disulphide bond in rabbit muscle phosphofructokinase].
A comparative study was performed for rabbit muscle phosphofructokinase (PFK) from normal and atherosclerotic animals. The diagonal electrophoretic technique was used for cysteic acid containing peptides separation. On performic acid oxidation among the tryptic peptides of PFK the disulphide containing peptide was found. Its electrophoretic mobility, compared to that of cysteic acid, gives ground for intrasubunit disulphied bond existence.
Animals↗
The reactivity of the thiol groups of the adenosine triphosphatase of sarcoplasmic reticulum and their location on tryptic fragments of the molecule.
The ATPase (adenosine triphosphatase) from sarcoplasmic reticulum contains 20 thiol groups/115000 daltons, measured by using either N-ethyl[(14)C]maleimide or 5,5'-dithiobis-(2-nitrobenzoate) in sodium dodecyl sulphate. After reduction there were 26 thiol groups, in good agreement with 26.5 residues of cysteic acid found by amino acid analysis. The difference between this and the 20 residues measured before reduction implies the presence of three disulphide residues. The same number of disulphide residues was found by direct measurement. Three to six fewer thiol groups were found in preparations made in the absence of dithiothreitol. The missing residues were accounted for as cysteic acid. The distribution of disulphide bonds and of exposed and buried thiol groups among the tryptic fragments of the molecule was measured after labelling with N-ethyl[(14)C]-maleimide. The disulphides were confined to fragment B (mol.wt. 55000), whereas several thiol groups were present on each of the fragments (A, B, A(1) and A(2)). The kinetics of the reaction of the ATPase with 5,5'-dithiobis-(2-nitrobenzoate) showed that four or five of the thiol groups were unreactive in the absence of detergent and that 13 of the remainder reacted with a single first-order rate constant. In the presence of ATP and Ca(2+) the reaction rate of all but two groups of this class was uniformly decreased. In the presence or absence of ATP and Ca(2+) the rate constant for inactivation was close to the rate constant for this class, but was not identical with it. No selective protection of a specific active-site-thiol group was observed. Parallel experiments with sarcoplasmic reticulum gave similar results, except that the reaction rates were a little lower and there were two more buried groups. Solution of ATPase of sarcoplasmic reticulum in detergent greatly increased the reactivity of all thiol groups. The effects of low concentrations of deoxycholate were reversible. EGTA or low concentrations (0.02mm) of Ca(2+) of Mg(2+) had very little effect on the reactivity.
Adenosine Triphosphatases↗
Axoplasm chemical composition in Myxicola and solubility properties of its structural proteins.
The chemical composition of axoplasm extracted from the giant axon of Myxicola infundibulum has been analysed, and some of the factors which disperse its gel structure have been identified. 2. The axoplasm contains about 3-6% protein, and 0-12% lipid. It is isosmotic with sea water and has a pH near 7-0. 3. Inorganic ions in extracted axoplasm include: Na+, 13m-mole/kg wet wtl; K+, 280; Cl-, 24; Ca2+, 0-3; Mg2+, 3. 4. Free organic ions in axoplasm include: gly, 180 m-mole/kg wet st.; cysteic acid, 120; asp, 75; glu, 10; ala, 7; tau, 5; thr, 2; gln and ser, trace; homarine, 63; isethionate, 0. 5. The gel structure is dispersed by solutions containing 1--10 mM-Ca2+, because this ion activates an endogenous protease. The gel can also be dispersed without proteilysis by solutions containing 0-5 M-KCl, or 0-5 M guanidine hydrochloride, or 3-5 M urea, all of which break down neurofilaments. 6. It is argued that many aspects of the composition and dispersal properties of Myxicola axoplasm are similar to those in other axons.
Amino Acids↗
[Utilization of inorganic sulfur sources by Staphylococcus aureus strains].
Staphylococcus aureus strains of different host-adapted variants (Meyer 1966) have been tested for their ability to use inorganic sulfur sources. All the 25 strains tested were able to utilize sodium sulfide as sulfur source in a medium similar to that described by Kloos and Pattee (1965). Using S. aureus strain 116/74 grown in a medium containing Na2-35S as the only sulfur source we studied incorporation and insertion of inorganic sulfide into sulfur containing amino acids. In disintegrated and fractionated cellular material we could find 35S labelled homocystine and methionine as major compounds, and cystine, cysteic acid, homocysteic acid, and beta-sulphopyruvate as minor compounds. The occurrence of homocystine and the sulfonic acids in bacterial proteins is rather uncommon.
Bacterial Proteins↗