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PubMed1985

[Thermodynamic and kinetic aspects of the hydrolysis of ethyl(R)-2- (benzyloxycarbonylamino)-3-sulfamoylpropionate in the presence of free and immobilized alpha-chymotrypsin].

The hydrolysis of ethyl (R)-2-(benzyloxycarbonylamino)-3-sulfamoylpropionate (blocked cysteic acid S-amide) by native and immobilized alpha-chymotrypsin was studied. The experiments were performed using a constant enzyme/substrate ratio of 1:8 and at a temperature of 10-40 degrees C; the immobilized enzyme was bound to a dialdehyde cellulose matrix. A kinetic equation (Eq.10) was found to be applicable which confirms that the mechanism of the enzyme reaction consists of several stages, irrespective of the enzyme state. The temperature dependence of the reaction velocity was investigated and applied using the Arrhenius equation. The constant value thus obtained for the activating energy showed that the active centres retained their character during immobilization. The differences between the velocities of the reaction with immobilized and with native enzyme corresponded to the different number of active centres during the reaction time. Based on these results a kinetic model of the mechanism of the studied reaction is presented which includes an initial balanced stage of the chemosorption type.

Adsorption↗
PubMed1995

Action of cystine in the cytotoxic response of Escherichia coli cells exposed to hydrogen peroxide.

Cystine markedly enhanced the cytotoxic response of Escherichia coli cells to concentrations of hydrogen peroxide resulting in mode one killing, but displayed little effect in mode two killed cells. The effect of cystine was concentration-dependent over a range of 5-50 microM and did not further increase at higher levels. Cystine had similar effects in other bacterial systems. In order to sensitize the cells to the oxidative injury, the amino acid must be present during exposure to the oxidant since no enhancement of the cytotoxic response can be observed in cystine pre-loaded cells. In addition, no further enhancement of cytotoxicity could be detected when cystine was added before and left during challenge with the oxidant. The enhancing effect of cystine on oxidative injury of E. coli cells appears to be directly mediated by the amino acid and in fact cysteic acid, the most likely oxidation product, had no effect on the killing of bacterial cells elicited by hydrogen peroxide. Other disulfide compounds such as oxidized glutathione, cystamine and dithionitrobenzoic acid only slightly increased the susceptibility of bacteria to the oxidant. The effect of the disulfides was not concentration-dependent over a range of 200-800 microM and was statistically significant only for cystamine. Taken together, these results indicate that cystine markedly increases the cytotoxic response of bacteria to hydrogen peroxide and suggest that the amino acid might impair the cellular defence machinery against hydrogen peroxide. This effect may involve a thiol-disulfide exchange reaction at the cell membrane level.

Cystine↗
PubMed1999

Effects of newly synthesized analogs of MIF-1 containing unnatural amino acids on electrically evoked smooth muscle contractions.

New MIF-1 (Pro-Leu-Gly-NH2) analogs containing unnatural amino acids such as L-canavanine (Cav) and L-cysteic acid S-(2-aminoethyl)amide (sLys) have been synthesized and in vitro experiments were performed to study their action on neurotransmission in target tissues with adrenergic and cholinergic neurotransmission. The experiments were carried out on electrically stimulated proximal guinea pig ileum (GPI) and the prostatic part of rat and rabbit vasa deferentia (VDR, VDRabb). The present results show that the newly synthesized Cav2-MIF and sLys2-MIF might affect electrically evoked smooth muscle contractions.

Adrenergic Agents↗
PubMed1982

[Amino acid sequence of seiwhale somatotropin].

Thirteen homogenous peptides were isolated from the chymotryptic hydrolysate of seiwhale somatotropin. The amino acid composition and sequence of the chymotryptic peptides were determined. Two large peptides were isolated from the tryptic hydrolysate of the performic acid-oxidized somatotropin. One of them had 20 amino acid residues and contained cysteic acid; the other one consisted of 31 residues and contained tryptophane and numerous leucine residues. The amino acid sequence of tryptic peptides was established after their hydrolysis with chymotrypsin. Based on these and earlier published data a complete amino acid sequence of seiwhale somatotropin comprising 190 amino acid residues was proposed. O comparison of primary structure of somatotropins from 6 different sources revealed the most conservative and variable regions of the hormone polypeptide chain.

Amino Acid Sequence↗
PubMed1975

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↗
PubMed2006

Kinetics and mechanisms of chlorine dioxide and chlorite oxidations of cysteine and glutathione.

Chlorine dioxide oxidation of cysteine (CSH) is investigated under pseudo-first-order conditions (with excess CSH) in buffered aqueous solutions, p[H+] 2.7-9.5 at 25.0 degrees C. The rates of chlorine dioxide decay are first order in both ClO2 and CSH concentrations and increase rapidly as the pH increases. The proposed mechanism is an electron transfer from CS- to ClO2 (1.03 x 10(8) M(-1) s(-1)) with a subsequent rapid reaction of the CS* radical and a second ClO2 to form a cysteinyl-ClO2 adduct (CSOClO). This highly reactive adduct decays via two pathways. In acidic solutions, it hydrolyzes to give CSO(2)H (sulfinic acid) and HOCl, which in turn rapidly react to form CSO3H (cysteic acid) and Cl-. As the pH increases, the (CSOClO) adduct reacts with CS- by a second pathway to form cystine (CSSC) and chlorite ion (ClO2-). The reaction stoichiometry changes from 6 ClO2:5 CSH at low pH to 2 ClO2:10 CSH at high pH. The ClO2 oxidation of glutathione anion (GS-) is also rapid with a second-order rate constant of 1.40 x 10(8) M(-1) s(-1). The reaction of ClO2 with CSSC is 7 orders of magnitude slower than the corresponding reaction with cysteinyl anion (CS-) at pH 6.7. Chlorite ion reacts with CSH; however, at p[H+] 6.7, the observed rate of this reaction is slower than the ClO2/CSH reaction by 6 orders of magnitude. Chlorite ion oxidizes CSH while being reduced to HOCl, which in turn reacts rapidly with CSH to form Cl-. The reaction products are CSSC and CSO3H with a pH-dependent distribution similar to the ClO2/CSH system.

Chlorides↗
PubMed1988

Prevention of acute gastric erosions in the rat by novel semi-synthetic amphipathic analogues of pepstatin.

Pepstatin is a potent aspartyl proteinase inhibitor which is virtually insoluble in physiological media. Five semi-synthetic amphipathic analogues of pepstatin, prepared by N terminal substitution of native pepstatin with hydrophilic oligopeptides, have been assessed for their ability to protect the mucosa in two animal models of acute gastric erosions. Concentrations of approximately 90 pmol/mg were achieved in the rat gastric mucosa after oral administration of a 20 mmol solution. These levels are theoretically adequate to inhibit all pepsin like proteinase activity (including zymogens). Each pepstatin analogue was tested by intragastric administration in a controlled hypotension/luminal acid animal model of acute gastric erosions in a group of six animals. All the inhibitors tested produced marked mucosal protection, as measured by a mucosal damage index, compared with control animals (control mean 241, range 100-420; Pepstatinyl-Gly-Orn-Orn-Cys (10 mmol) mean 3, range 0-8, p less than 0.01; Pepstatinyl-Gly-Cysteic acid-Cysteic acid (10 mmol) mean 5, range 0-21, p less than 0.01; Pepstatinyl-Gly-Lys-Lys (10 mmol) mean 18, range 0-60, p less than 0.01; Pepstatinyl-Gly-Cysteic acid-Cysteic acid (1 mmol) mean 24, range 0-86, p less than 0.01; Pepstatinyl-Gly-Orn-Orn-Cys (1 mmol) mean 57, range 0-116, p less than 0.01; Pepstatinyl-Gly-Asp-Asp (1 mg/ml suspension) mean 68, range 19-126, p less than 0.01; Pepstatinyl-Arg-OMe (1 mmol) mean 93, range 4-142, p less than 0.05, Pepstatinyl-Gly-Lys-Lys (1 mmol) mean 157, range 70-286, NS). In a platelet activating factor/20% luminal ethanol model of erosions the pepstatin analogues again provided mucosal protection although this only reached statistical significance for one of three compounds tested.

Animals↗
PubMed1990

Autoradiographic characterization of putative excitatory amino acid transport sites.

Removal of excitatory amino acids from the extracellular space is now postulated to occur through at least two distinct transport systems that are distinguished by their ionic dependency. Thus, both sodium-dependent and chloride-dependent systems have been described in the mammalian central nervous system. In this report we attempt to characterize these sites by autoradiography, using D-[3H]aspartate and L-[3H]glutamate as ligands. Previous studies have shown that sequestration of radioligand into membrane vesicles can be a potential artifact when examining transport sites. We have found that sequestration can be alleviated by incubation of tissue sections in xylenes prior to incubation with radioligand. Using in vitro autoradiography we have characterized the two binding sites with respect to their distribution, kinetics and pharmacology. Both appeared to have a single, saturable binding site with Kds in the low micromolar range. Sodium-dependent D-aspartate binding predominated, having a Bmax that was five times greater than chloride-dependent L-glutamate binding in whole brain. The levels of binding to the two sites varied between brain regions. Sodium-dependent D-aspartate binding was highest in the cerebellar molecular layer greater than dentate gyrus molecular layer greater than entorhinal cortex. Chloride-dependent L-glutamate binding was highest in the outer layers of cerebral cortex greater than dentate gyrus molecular layer greater than entorhinal cortex greater than striatum. Pharmacological characterization of these sites also showed major differences. Sodium-dependent D-aspartate binding was most potently inhibited by L-aspartate greater than threo-beta-hydroxyaspartate greater than L-cysteine sulfinic acid greater than L-cysteic acid. Chloride-dependent glutamate binding was most potently inhibited by L-glutamate greater than L-alpha-amino adipic acid greater than quisqualate greater than L-serine-o-sulfate. The differences in distribution, ligand binding properties and pharmacology of these sites suggest that a significant variable in excitatory amino acid circuitry may include heterogeneity in transporters associated with excitatory pathways.

Amino Acids↗
PubMed2001

Dissociation of multiply charged negative ions for hirudin (54-65), fibrinopeptide B, and insulin A (oxidized).

Collision-induced dissociation (CID) was performed on multiply deprotonated ions from three commercial peptides: hirudin (54-65), fibrinopeptide B, and oxidized insulin chain A. Ions were produced by electrospray ionization in a Fourier transform ion cyclotron resonance mass spectrometer. Each of these peptides contains multiple acidic residues, which makes them very difficult to ionize in the positive mode. However, the peptides deprotonate readily making negative ion studies a viable alternative. The CID spectra indicated that the likely deprotonation sites are acidic residues (aspartic, glutamic, and cysteic acids) and the C-terminus. The spectra are rife with c, y, and internal ions, although some a, b, x, and z ions form. Many of the fragment ions were formed from cleavage adjacent to acidic residues, both N- and C-terminal to the acidic site. In addition, neutral loss (e.g., NH3, CH3, H2O, and CO2) was prevalent from both the parent ions and from fragment ions. These neutral eliminations were often indicative of specific amino acid residues. The fragmentation patterns from several charge states of the parent ions, when combined, provide significant primary sequence information. These results suggest that negative mode CID of multiply deprotonated ions provides useful structural information and can be worthwhile for highly acidic peptides that do not form positive ions in abundance.

Amino Acid Sequence↗
PubMed1997

Affinity cleavage at the metal-binding site of phosphoenolpyruvate carboxykinase.

Chicken liver phosphoenolpyruvate carboxykinase (PEPCK) was rapidly inactivated by micromolar concentrations of ferrous sulfate in the presence of ascorbate at pH 7.4. Omitting ascorbate or replacing the Fe2+ with Mn2+ or Mg2+ gives no inactivation. Mn2+, Mg2+, or Co2+ at 100-fold molar excess over Fe2+ offered complete protection from Fe2+/ascorbate-induced inactivation. The substrates PEP and GTP, but not OAA, GDP, or CO2, offered full protection from inactivation. The addition of 5 mM EDTA stopped further inactivation of the enzyme. Thermodynamic studies indicate that the inactive enzyme no longer binds Mn2+ but still had high affinity for GTP indicating that the inactivation process was specific for the metal site. A decrease in cysteine content was observed over time following PEPCK treatment with Fe2+ and ascorbate. The apparent first-order rate constant for free sulfhydryl loss (0.085 +/- 0.005 min-1) is similar to the apparent first-order rate constant for inactivation (0.067 +/- 0.005 min-1). Amino acid composition analysis revealed that cysteic acid was generated upon Fe2+/ascorbate addition to PEPCK. Native chicken liver PEPCK has an Mr of 67 kDa. SDS-PAGE of the inactivated enzyme showed the presence of two new bands at 31.7 and 35.3 kDa indicating that PEPCK was specifically cleaved at a single site. The rate of cleavage was slower than the rate of inactivation and fully inactivated enzyme was only 50% cleaved. The Fe2+/ascorbate-catalyzed inactivation was not solely due to protein cleavage. The protein fragments generated by cleavage were separated by C4 reverse phase HPLC. The cleavage exposed a new N-terminus which was identified to be the 35.3 kDa C-terminal half of PEPCK. Sequencing of the fragments indicated that the site of cleavage was between Asp296 and Ile297. These results indicate that Asp296 is involved in metal chelation. This agrees with previous studies [Hlavaty, J. J., & Nowak, T. (1997) Biochemistry 36, 3389-3403] that suggested that Asp295 and Asp296 are involved in metal binding.

Amino Acid Sequence↗
PubMed1981

Amino acid transport in Myxicola giant axon: stability of the amino acid pool, taurine efflux, and trans effect of sodium.

1. The giant axon of Myxicola infundibulum was assessed for its suitability as a model preparation for study of amino acid transport mechanisms.2. The amino acid composition of axoplasm was measured and compared with those of coelomic fluid, muscle and axon sheath. The axoplasmic composition is unique. Axoplasm/coelomic fluid concentration ratios are all much larger than 1. The axoplasmic amino acid concentrations are (mmol/kg plasm): cysteic acid (104), aspartic acid (75), glutamic acid (10), taurine (64), serine (5), glycine (191) and alanine (5). Other amino acids or primary amines, if present, must have concentrations of less than 1 mm.3. The size of the sheath amino acid pool is 12% or less of the axoplasmic pool.4. The amino acid pool of axons soaked in sea water for up to 24 h is stable. Removal of Na from sea water causes a large increase of net efflux and net production of amino acids.5. Net amino acid production can not be detected in sheath. Metabolic production occurs in axoplasm with little accumulation. Time scales for production and net efflux are therefore similar.6. The Myxicola axon has a vigorous amino acid metabolism and transport systems capable of relatively large fluxes. Homeostasis is strongly linked to Na and may involve Na-coupled co-transport. Conservation of transmembrane amino acid gradients could be promoted in part by trans inhibition of efflux by external Na.7. Taurine is a useful model substrate because it is not catabolized in Myxicola and its net efflux is sensitive to Na. [(3)H]taurine efflux was measured from injected axons. Fluxes and internally recorded action potentials are stable for up to 6 h.8. Axon sheaths take up [(3)H]taurine from 10 mm-taurine sea water with an apparent half-time of 5 h. [(3)H]taurine washout from the apparent extracellular space has a half-time of 5 min. Washout from sheath cells has a half-time of 2-3 h. Sheath is not an important parallel compartment for taurine fluxes in the axon.9. Taurine efflux has a Q(10) of 1.8.10. Taurine efflux is insensitive to external taurine concentrations up to 10 mm.11. Taurine efflux is sensitive to external Na, but only if internal Na is high.12. Taurine is transported by a low-affinity Na-dependent system in Myxicola axon. Results could be explained by a carrier which is more mobile in the empty state than in the substrate-loaded state. Trans inhibition of taurine efflux by external Na is an important property of the system, and contributes to conservation of axoplasmic taurine.

Action Potentials↗
PubMed1984

Localization of cysteine sulfinic acid uptake sites in rat brain by quantitative autoradiography.

In vitro autoradiography was employed to localize and quantify Na-dependent binding sites of [35S]cysteic acid (CA), an analog of cysteine sulfinic acid (CSA). The heterogeneous anatomical distribution and pharmacological specificity of [35S]CA differs from that of the glutamate/aspartate marker D-[3H]aspartate, and appears to represent a specific uptake site for CSA. These results suggest that CSA may act as an excitatory transmitter in the central nervous system.

Amino Acids, Sulfur↗
PubMed1989

Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment membrane proteins. Evidence for methyl ester formation at carboxyl-terminal cysteinyl residues.

A group of 23-29-kDa polypeptides in the membranes of bovine rod outer segments are substrates for S-adenosylmethionine-dependent methylation reactions. The bulk of the methyl group incorporation is in base-labile ester-like linkages, and does not appear to be due to the widespread D-aspartyl/L-isoaspartyl methyltransferase (EC 2.1.1.77). To determine the site(s) of methylation, 3H-methylated proteins separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate were eluted and digested with papain, leucine aminopeptidase-M, and prolidase. After performic acid oxidation of the digest, a base-labile radioactive material was recovered that coeluted with a synthetic standard of cysteic acid methyl ester upon cation exchange and G-15 gel filtration chromatography, as well as in two thin-layer electrophoresis and two thin-layer chromatography systems. These results provide direct evidence for the methylation of the alpha-carboxyl group of a carboxyl-terminal cysteinyl residue, a modification that has been proposed for the 21-kDa Ha-ras product and other cellular proteins (Clarke, S., Vogel, J. P., Deschenes, R. J., and Stock, J. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 4643-4647).

Amino Acid Sequence↗
PubMed1977

[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↗
PubMed1983

[Enzymatic synthesis of taurine].

In view of its interesting pharmacological and physiological functions, the enzymic synthesis of the taurine or the beta-aminoethan- alpha-sulfonic acid is described. This compound has been prepared by decarboxylation with rat heart homogenate and at room temperature of cysteic acid obtained by KMnO4 cysteine oxidation. The taurine prepared has been identified by paper and thin-layer chromatography with a taurine pure sample.

Animals↗
PubMed1975

Inactivation of Salmonella phosphoribosylpyrophosphate synthetase by oxidation of a specific sulfhydryl group with potassium permanganate.

Phosphoribosylpyrophosphate synthetase from Salmonella typhimurium contains four cysteine residues per subunit. Three of these react readily with 5, 5'-dithiobis(2-nitrobenzoic acid) (DTNB), forming an active derivative with kinetic and physical properties similar to the native enzyme, but one reacts only under denaturing conditions. Stoichiometric amounts of KMnO4 inactivate the DTNB-treated enzyme. The loss of activity is correlated with the oxidation of the remaining cysteinyl group to cysteic acid by KMnO4. Amino acid analysis indicates that no other residues are altered. The rate of inactivation of the enzyme is decreased 30-fold by saturatin g concentrations of the substrate ATP. Inorganic phosphate also protects substantially against KMnO4. Titration of the native enzyme with limiting amounts of KMnO4 shows that the sulfhydryl group essential for activity competes effectively with the other sulfhydryl groups for KMnO4. These results suggest that the essential sulfhydryl group is near the active site, and that KMnO4, a phosphate analogue, can act as an active site-directed reagent at the ATP binding site of the enzyme. The KMnO4-oxidized enzyme is more highly aggregated than untreated enzyme and fails to bind ATP appreciably.

Adenosine Diphosphate↗
PubMed2005

Changing the specificity of a bacterial chemoreceptor.

The methyl-accepting chemotaxis proteins are a family of receptors in bacteria that mediate chemotaxis to diverse signals. To explore the plasticity of these proteins, we have developed a simple method for selecting cells that swim to target attractants. The procedure is based on establishing a diffusive gradient in semi-soft agar plates and does not require that the attractant be metabolized or degraded. We have applied this method to select for variants of the Escherichia coli aspartate receptor, Tar, that have a new or improved response to different amino acids. We found that Tar can be readily mutated to respond to new chemical signals. However, the overall change in specificity depended on the target compound. A Tar variant that could detect cysteic acid still showed a strong sensitivity to aspartate, indicating that the new receptor had a broadened specificity relative to wild-type Tar. Tar variants that responded to phenylalanine or N-methyl aspartate, or that had an increased sensitivity to glutamate showed a strong decrease in their response to aspartate. In at least some of the cases, the maximal level of sensitivity that was obtained could not be attributed solely to substitutions within the binding pocket. The new tar alleles and the techniques described here provide a new approach for exploring the relationship between ligand binding and signal transduction by chemoreceptors and for engineering new receptors for applications in biotechnology.

Amino Acid Sequence↗