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PubMed1991

Purification and characterization of a new NAD(+)-dependent enzyme, L-tartrate decarboxylase, from Pseudomonas sp. group Ve-2.

A new enzyme, L-tartrate decarboxylase, was found in cells of Pseudomonas sp. group Ve-2. The enzyme was purified to homogeneity and characterized. The enzyme requires K+, Mg2+, and NAD+ for L-tartrate decarboxylation. The dependence of the enzymatic decarboxylation on NAD+ suggests that the decarboxylation involves redox reactions of the substrate. The enzyme catalyzes NAD(+)-linked oxidative decarboxylation of D-malate as well. The enzyme is composed of four subunits with identical molecular weight (Mr 40,000). The apparent Michaelis constants for L-tartrate and NAD+ are 1.1 mM, respectively. The cofactor requirements and the physical properties of the enzyme were similar to those of L-tartrate dehydrogenase-D-malate dehydrogenase from Rhodopseudomonas sphaeroides, and tartrate dehydrogenase from P. putida.

Carboxy-Lyases↗
PubMed1999

Effect of elevated temperature and light on the stability of butorphanol tartrate.

The purpose of this investigation was to determine the short-term stability of butorphanol tartrate in presence of diluents. A 10-mg/mL solution of butorphanol tartrate was diluted to 5 mg/mL using normal saline, 5% dextrose in water (D5W), or sterile water for injection. The diluted solutions were divided into two groups. The effect of temperature was tested by placing one group of sealed amber vials at room temperature and at 37 degrees C. The effect of light was studied by placing a second group in amber and clear vials, then exposing them directly to light. At regular time intervals over a period of 5 weeks, the solutions were analyzed for butorphanol tartrate and degradation products using a high-performance liquid chromatography assay. The concentration of butorphanol tartrate remained practically unchanged, indicating that butorphanol tartrate is not affected by heat or light in the presence of any of the diluents over a period of 5 weeks.

Butorphanol↗
PubMedDate not supplied

Randomized, double-blind comparison of acute beta1-blockade with 50 mg metoprolol tartrate vs 25 mg carvedilol in normal subjects.

Differential efficacy of immediate-release metoprolol tartrate and carvedilol in the treatment of congestive heart failure remains a subject of ongoing debate. The degree of beta1-blockade can be assessed by percentage reduction of exercise heart rate. Twelve healthy subjects underwent symptom-limited cardiopulmonary exercise testing repeated weekly and 2 hours after randomized, double-blind administration of 50 mg metoprolol tartrate vs 25 mg carvedilol. Baseline heart rate, heart rate at 40% and 70% peak O2 consumption, and maximal exercise were significantly blunted more by metoprolol tartrate than by carvedilol (P<.05 for all). Peak O2 consumption was significantly reduced by metoprolol tartrate (P<.03) but not by carvedilol (P=.054). The change in O2 consumption was significantly correlated with the degree of beta1-blockade (r =0.45; P<.05). In healthy subjects, a higher degree of beta1-blockade is achieved with 50 mg metoprolol tartrate compared with 25 mg carvedilol.

Adrenergic alpha-Antagonists↗
PubMed1993

Stability of metoprolol tartrate in 5% dextrose injection or 0.9% sodium chloride injection.

The stability of metoprolol tartrate 0.40 mg/mL in 5% dextrose injection or 0.9% sodium chloride injection in polyvinyl chloride (PVC) bags stored at 24.0 +/- 2.4 degrees C was studied. Triplicate admixtures of each solution were prepared. A stability-indicating high-performance liquid chromatographic assay was used to determine metoprolol tartrate concentrations. At 0, 6, 12, 24, and 36 hours, samples were visually assessed then assayed in duplicate. Stability was defined as a < 10% decline in metoprolol tartrate concentration from the time 0 determination. No notable color changes or precipitation was observed in any sample. All samples demonstrated a < 7% reduction in metoprolol tartrate concentration over 36 hours. Metoprolol tartrate 0.40 mg/mL admixed in 5% dextrose injection or 0.9% sodium chloride injection in PVC bags and stored at 24.0 +/- 2.4 degrees C was stable for 36 hours.

Chromatography, High Pressure Liquid↗
PubMed1985

Tartrate-resistant acid phosphatase staining of monocytes in Gaucher disease.

Cytochemical studies were performed on peripheral blood from 30 patients with type 1 Gaucher disease. In 29 of the patients, peripheral blood monocytes stained positively for tartrate-resistant acid phosphatase, whereas monocytes from 18 normal individuals and 14 patients with monocytosis did not. In the Gaucher patients, the percentage of monocyte positivity for tartrate-resistant acid phosphatase ranged from 2 to 97. There was no correlation between the percent monocyte staining and the degree of disease severity, as measured by hepatosplenomegaly, pancytopenia, or extent of bone disease, for the group as a whole. In Gaucher patients who had not undergone splenectomy, however, there was a significant correlation between percent monocyte staining and the degree of hepatosplenomegaly, anemia, and thrombocytopenia. The presence of tartrate-resistant acid phosphatase may be secondary to the lysosomal accumulation of glucosyl ceramide within these monocytes, although this remains to be confirmed. If so, these circulating cells may represent precursors of the Gaucher cells in tissues. Tartrate-resistant acid phosphatase staining of peripheral blood monocytes may be useful as a diagnostic marker for Gaucher type 1 disease and for further studies on the pathogenesis of the disease.

Acid Phosphatase↗
PubMed1989

Ultrastructural localization of tartrate-resistant, purple acid phosphatase in rat osteoclasts by histochemistry and immunocytochemistry.

The intracellular localization of the tartrate-resistant purple acid phosphatase in osteoclasts of developing rat bone has been determined immunocytochemically using an antiserum to the purified bone-derived purple acid phosphatase. The localization of the immunoreactivity was compared with the results of enzyme histochemistry using p-nitrophenylphosphate as substrate and 10 mM tartrate. Both methods revealed the presence of the enzyme in numerous vesicles of various sizes up to 2-3 microns in diameter and in granules. There was no immunoreactivity in the Golgi apparatus, and tartrate completely inhibited the histochemical activity of this organelle. No consistent extracellular activity could be detected, nor was any reaction product observed at the ruffled border. The localization of the tartrate-resistant purple acid phosphatase in osteoclasts is consistent with an intracellular function for this enzyme.

Acid Phosphatase↗
PubMed1980

Solubility and dissolution rate studies of ergotamine tartrate.

The solubility of ergotamine tartrate in aqueous solutions of tartaric acid, citric acid, hydrochloric acid, and caffeine and the dissolution rate of ergotamine tartrate in aqueous mixtures containing hydrochloric acid, caffeine, citric acid, or sodium acetate were studied. The Noyes-Whitney model of dissolution is useful for predicting the dissolution rate of ergotamine tartrate in most of the dissolution media. The relative slowness with which ergotamine chloride (a substance with low water solubility) precipitated when ergotamine tartrate was dissolved in 0.1 M HCl resulted in the solid dissolving faster in this medium than was predicted using the Noyes-Whitney equation.

Caffeine↗
PubMed1994

Anaerobic growth of Salmonella typhimurium on L(+)- and D(-)-tartrate involves an oxaloacetate decarboxylase Na+ pump.

We show here that the Enterobacterium Salmonella typhimurium LT2 has the capacity to grow anaerobically on L(+)- or D(-)-tartrate as sole carbon and energy source. Growth on these substrates was Na(+)-dependent and involved the L(+)- or D(-)-tartrate-inducible expression of oxaloacetate decarboxylase. The induced decarboxylase was closely related to the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae as shown by the sensitivity towards avidin, the location in the cytoplasmic membrane, activation by Na+ ions, and Western blot analysis with antiserum raised against the K. pneumoniae oxaloacetate decarboxylase. Participation of an oxaloacetate decarboxylase Na+ pump in L(+)-tartrate degradation by S. typhimurium is in accord with results from DNA analyses. The deduced protein sequence of the open reading frame identified upstream of the recently sequenced oxaloacetate decarboxylase genes is clearly homologous with the beta-subunit of L-tartrate dehydratase from Escherichia coli. Southern blot analysis with S. typhimurium chromosomal DNA indicated the presence of probably more than one gene for oxaloacetate decarboxylase.

Amino Acid Sequence↗
PubMed2006

Parasite field study in central Kentucky on thoroughbred foals (born in 2004) treated with pyrantel tartrate daily and other parasiticides periodically.

Foals (79), born in 2004 on three thoroughbred horse farms (C, M, and S) in central Kentucky, were fed pyrantel tartrate daily, beginning at about 3 months of age. In addition, other parasiticides [fenbendazole (FBZ), ivermectin (IVM) alone or with praziquantel (PRAZ), oxibendazole (OBZ), pyrantel pamoate (PRT), and moxidectin (MOX)] were given periodically. All treatments were administered by farm personnel. Over a 14-month period, from May 2004 to July 2005, collections (n=989) of feces were made from the foals for determination of presence of internal parasite eggs/oocysts by qualitative and/or quantitative methods. Conclusions on drug activity are based necessarily on considering the combined effect of pyrantel tartrate and the other compounds. For small strongyles, this was related to which specific additional compound was given. Based on the percentage of foals with strongyle-egg-positive feces and/or the level of eggs per gram of feces (EPG) counts for the foals after treatment, drug activity on small strongyles was highest to lowest for MOX, IVM and IVM/PRAZ, FBZ, OBZ, PRT, and FBZ (2x for 5 days). The macrocyclic lactones (MOX and IVM) were highly superior to the other compounds. Some of the strongyle counts were high (over 2,000), especially on one farm (S), during periods when foals received only pyrantel tartrate, but a few days after administration of therapeutic dose rates of the drugs IVM or MOX, they were negative or very low. Ascarid eggs were present in feces of three foals after treatment with a combination of IVM and PRAZ. The qualitative method was more efficient than the quantitative method in detection of ascarid and strongyle eggs in the feces. Prevalence of eggs of ascarids (Parascaris equorum) was low (0, 4, and 31%), of strongyles high (80, 100, and 100%), of Strongyloides westeri very low (only one infected foal), and oocysts of Eimeria leuckarti medium to high (36, 41, and 85%) for the three farms, C, M, and S, respectively. It is uncertain whether the low ascarid prevalence was from activity of pyrantel tartrate and/or the other drugs or to a limited source of infective eggs.

Animals↗
PubMed2006

The safety and intraocular pressure-lowering efficacy of brimonidine tartrate 0.15% preserved with polyquaternium-1.

PURPOSE: The safety and intraocular pressure (IOP)-lowering efficacy of brimonidine tartrate 0.15% preserved with polyquaternium-1 were evaluated and compared with brimonidine tartrate 0.15% preserved with chlorine dioxide in patients with open-angle glaucoma (OAG) or ocular hypertension (OHT). DESIGN: Randomized, double-masked, parallel group, multicenter equivalence study. PARTICIPANTS: Eight hundred forty-two patients randomized to the study treatments. METHODS: Patients with OAG or OHT and with qualifying IOP (22-36 mmHg at 8 am on 2 eligibility visits after an appropriate washout period from previous treatment) were assigned randomly to either brimonidine tartrate 0.15% preserved with polyquaternium-1 (brimonidine PQ) or brimonidine tartrate 0.15% preserved with chlorine dioxide (brimonidine P) dosed 3 times daily and were followed up for 6 months. Approximately one half of the study sites continued to follow up their patients for an additional 6 months to obtain longer-term safety data. RESULTS: Brimonidine PQ produced statistically significant and clinically relevant reductions from baseline ranging from 4.3 to 6.5 mmHg, which were statistically and clinically equivalent to brimonidine P at all 18 visit days and times. No safety concerns were identified based on an assessment of ocular and cardiovascular parameters. Patient discontinuations resulting from adverse events were similar for both groups and most of these were a result of signs or symptoms of ocular allergic reaction. CONCLUSIONS: Brimonidine PQ is equivalent in IOP-lowering efficacy and safety to brimonidine P.

Adrenergic alpha-Agonists↗
PubMed1998

Twelve-month results of an ongoing randomized trial comparing brimonidine tartrate 0.2% and timolol 0.5% given twice daily in patients with glaucoma or ocular hypertension. Brimonidine Study Group 2.

OBJECTIVE: To compare the long-term safety and ocular-hypotensive efficacy of brimonidine tartrate 0.2% with timolol maleate 0.5% administered twice daily in patients with glaucoma or ocular hypertension. DESIGN: A double-masked, parallel-group, active-controlled, multicenter clinical trial of 12 months' duration. PARTICIPANTS: Four hundred eighty-three patients with glaucoma or ocular hypertension were enrolled. Of these, 463 were evaluated according to the protocol criteria (280 in the brimonidine tartrate group and 183 in the timolol group). INTERVENTIONS: Brimonidine tartrate 0.2% or timolol maleate 0.5% was administered twice daily. MAIN OUTCOME MEASURES: The primary efficacy variable was intraocular pressure (IOP). RESULTS: Brimonidine and timolol produced significant (P < 0.001) and sustained mean reductions in IOP throughout the 1-year follow-up when measured at hour 0 (trough) and at hour 2 (peak). At weeks 1 and 2 and month 12, significantly greater mean decreases in IOP measured at peak (P < or = 0.007) were observed in patients treated with brimonidine as compared to timolol, whereas the mean decreases in IOP measured at trough was significantly greater in patients treated with timolol as compared to brimonidine (P < 0.001) at all follow-up visits. Both drugs were well-tolerated. The incidence of adverse events was similar in both treatment groups, except for ocular allergy, oral dryness, and conjunctival follicles, which occurred more frequently in the brimonidine group, and burning-stinging, which occurred more frequently in the timolol group. Patients receiving timolol experienced significant decreases in heart rate at all follow-up visits. CONCLUSIONS: Topically applied twice daily for 12 months, brimonidine tartrate 0.2% was safe and effective in lowering IOP in patients with glaucoma or ocular hypertension.

Adrenergic alpha-Agonists↗
PubMed1994

The specific inhibition of crystal growth of monohydrogen potassium L-tartrate by d-catechin.

Crystal growth of monohydrogen potassium L-tartrate in an ethanolic aqueous solution was specifically inhibited by d-catechin, but not by either its epimeric isomer at C3, l-epicatechin or by gallic acid and caffeic acid. 3D-Structure similarity search of d-catechin with two molecules of the tartrate and docking study of d-catechin with the crystal model of the tartrate suggested that d-catechin mimics a structure consisting of the two tartrate molecules in the inhibition. Differences in the conformation of the catechol moieties of d-catechin and l-epicatechin may explain the distinct inhibitory effects of the epimeric isomers.

Catechin↗
PubMed1995

Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions.

The substrate specificity of tartrate dehydrogenase has been probed using a series of alternative substrates to identify the molecular interactions which determine whether a particular substrate undergoes enzyme-catalyzed decarboxylation or not. A series of 3-substituted malate analogs, in which F, Cl, Br, I, SH, or NH2 substituents were placed at the 3R- or 3S-position, was prepared, and the product resulting from the action of tartrate dehydrogenase on each compound was identified. All of the halomalates and both diastereomers of aminomalate underwent oxidative decarboxylation; both diastereomers of 3-thiomalate underwent net nonoxidative decarboxylation. The results were interpreted in terms of a model in which decarboxylation is conformationally controlled. The data are not consistent with a model which suggests that substrates assume the conformation that is necessary to avoid steric crowding between the enzyme and the substituent at the 3-position of the substrate. These data are consistent with a model in which the course of the reaction with (+)-tartrate and meso-tartrate is dictated by the coordination of the substrate hydroxyls to the active site Mn2+. However, the observed reactivities of the 3-methyltartrate diastereomers are not consistent with this model, either: (2R,3R)-3-methyltartrate undergoes oxidative decarboxylation, and (2R,3S)-3-methyltartrate undergoes simple oxidation. These results suggest that for these compounds the conformation is dictated by the positioning of the hydrophobic substituent in a specific binding pocket.(ABSTRACT TRUNCATED AT 250 WORDS)

Alcohol Oxidoreductases↗
PubMed1999

Action potential conduction block of nerves in vitro by potassium citrate, potassium tartrate and potassium oxalate.

OBJECTIVES: Potassium salts in desensitising formulations are believed to act by blocking nerve conduction. The aim of this study was to assess the ability of some organic potassium salts to block action potential conduction and to compare their effects with potassium chloride and potassium nitrate. MATERIALS AND METHOD: Potassium citrate, oxalate or tartrate were added to Krebs' solutions to raise the potassium concentration to 8-64 mM. The test solutions were applied to rat spinal nerves in a bath while monitoring the compound action potentials evoked by electrical stimulation. RESULTS: All potassium salts attenuated the compound action potential in a dose-dependent manner. There were no significant differences between the effects of potassium tartrate and potassium citrate solutions (p>0.1) which caused significantly greater compound action potential attenuation than the same concentrations of potassium oxalate (p<0.05). On the basis of the potassium ion concentration required to cause 50% attenuation of the compound nerve action potential, the relative potencies of the potassium salts were: citrate = tartrate> oxalate>chloride =nitrate. CONCLUSION: Potassium citrate and potassium tartrate were more effective than other potassium salts in blocking nerve conduction and may be more effective dentinal desensitising agents.

Action Potentials↗
PubMed1975

Unidirectional inhibition and activation of "malic' enzyme of Solanum tuberosum by meso-tartrate.

A kinetic study of "malic' enzyme (EC 1.1.1.40) from potato suggests that the mechanism is Ordered Bi Ter with NADP+ binding before malate, and NADPH binding before pyruvate and HCO3-. The analysis is complicated by the non-linearity that occurs in some of the plots. meso-Tartrate is shown to inhibit the oxidative decarboxylation of malate but to activate the reductive carboxylation of pyruvate. To explain these unidirectional effects it is suggested that the control site of "malic' enzyme binds organic acids (including meso-tartrate) which activate the enzyme. meso-Tartrate, however, competes with malate for the active site and thus inhibits the oxidative decarboxylation of malate. Because meso-tartrate does not compete effectively with pyruvate for enzyme-NADPH, its binding at the control site leads to a stimulation of the carboxylation of pyruvate. A similar explanation is advanced for the observation that malic acid stimulates its own synthesis.

Bicarbonates↗
PubMed1996

Inhibition of Salmonella typhimurium by the products of tartrate metabolism by a Veillonella species.

The inhibition of the growth of Salmonella typhimurium by a Veillonella species grown on media supplemented with tartrate was examined. Growth of Salmonella typhimurium was not inhibited by the concentrations of products metabolized by Veillonella cultures on media supplemented with 0 or 50 mmol l-1 of tartrate, but was inhibited on media supplemented with 100 or 150 mmol l-1 of tartrate. Inhibition of Salm. typhimurium was correlated with the increased production of acetate and propionate from tartrate by the Veillonella species.

Acetates↗
PubMed1987

Tartrate-resistant acid phosphatase in bone and cartilage following decalcification and cold-embedding in plastic.

Tartrate-resistant acid phosphatase (TRAP) has been proposed as a cytochemical marker for osteoclasts. We have developed an improved technique for the localization of TRAP in rat and mouse bone and cartilage. This procedure employs JB-4 plastic as the embedding medium, permits decalcification, and results in improved morphology compared with frozen sections. Peritoneal lavage cells were used to determine the appropriate isomer and concentration of tartrate necessary for inhibition of tartrate-sensitive acid phosphatase. After incubation in medium containing 50 mM L(+)-tartaric acid, osteoclasts and chondroclasts were heavily stained with reaction product. On the basis of their relative sensitivity to tartrate inhibition, three populations of mononuclear cells could also be distinguished. These three populations may represent: heavily stained osteoclast/chondroclast precursors; sparsely stained osteoblast-like cells lining the bone surface; and unstained cells of monocyte-macrophage lineage. Our results are consistent with the use of TRAP as a histochemical marker for study of the osteoclast.

Acid Phosphatase↗
PubMed1984

Tartrate-inhibitable acid phosphatase. Purification from placenta, characterization and subcellular distribution in fibroblasts.

Tartrate-inhibitable acid phosphatase was purified to apparent homogeneity from human placenta. The enzyme is composed of two subunits with an apparent molecular mass of 48 kDa. Each subunit carries one oligosaccharide of the high-mannose/hybride type. The purified enzyme has an isoelectric point of pH 6.2. It cleaves phosphomonoester bonds at acid pH, is competitively inhibited by L-tartrate, Ki = 0.51 microM, and phosphate, Ki = 0.8mM. A monospecific antiserum raised against the purified placental enzyme precipitated 62% and 85% of the tartrate-inhibitable acid phosphatase present in extracts of placenta and fibroblasts, respectively. By means of subcellular fractionation and immunoprecipitation it was shown that the majority of tartrate-inhibitable acid phosphatase is located in lysosomes in normal and mucolipidosis II fibroblasts. In the human Hep G-2 hepatoma cells a significant fraction of the enzyme appears to be associated with non-lysosomal organelles.

Acid Phosphatase↗