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PubMed1988

A possible mechanism on the potentiating vascular effect of coadministration of ifenprodil tartrate and calcium hopantenate: a study in the internal carotid artery.

Recently, it has been proposed that the combined administration of ifenprodil tartrate and calcium hopantenate might produce a beneficial synergistic effect in the treatment of cerebrovascular diseases. To further examine this clinical phenomena, the blood flow in the internal carotid arteries of the rat and the isometric tension of canine internal carotid arteries were measured with a transit-time ultrasonic volume flowmeter and a force transducer, respectively. Ifenprodil tartrate produced a sustained increase in the internal carotid arterial blood flow of rats, while calcium hopantenate had no effect. However, the increase in the internal carotid arterial blood flow induced by ifenprodil tartrate was significantly enhanced by calcium hopantenate. Ifenprodil tartrate caused a dose-related relaxation of K+-induced contractions in the isolated canine internal carotid arteries, while calcium hopantenate had no effect. The dose-response curve of ifenprodil tartrate was shifted to the left by pre-incubation in calcium hopantenate. Ifenprodil tartrate inhibited the K+-induced Ca2+ uptake in the canine internal carotid arteries, and the inhibition induced by ifenprodil tartrate was significantly enhanced by calcium hopantenate. These results suggest that the observed enhancement by calcium hopantenate of the ifenprodil tartrate effect on the internal carotid arterial blood flow was due to increased vascular myorelaxation resulting from the influence of calcium hopantenate on the Ca2+ movement.

Animals↗
PubMed1988

A possible mechanism on the potentiated vascular effect of coadministration of ifenprodil tartrate and calcium hopantenate: a study in the basilar and vertebral arteries.

In our earlier report [Shibuya et al. in press], we demonstrated the partial mechanism of the synergism between ifenprodil tartrate and calcium hopantenate on cardiovascular diseases. The mechanisms of the synergistic effects in the basilar and vertebral arteries were further studied in this paper using our described methods. Ifenprodil tartrate produced a sustained increase in the vertebral arterial blood flow of rats, while calcium hopantenate. Ifenprodil tartrate caused dose-related relaxation of K+-induced contractions in by ifenprodil tartrate was significantly enhanced by the coadministration of calcium hopantenate. Ifenprodil tartrate caused dose-related relaxation of K+-induced contractions in isolated canine basilar arteries, while calcium hopantenate had no effect. The dose-relaxation curve of ifenprodil tartrate was shifted to the left by pre-incubation in calcium hopantenate. In K+-depolarized basilar arteries, ifenprodil competitively antagonized the response to Ca2+, and this was enhanced by pre-incubation in calcium hopantenate. Ifenprodil tartrate inhibited K+-induced Ca2+ uptake in canine cerebral arteries and this was enhanced by pre-incubation in calcium hopantenate. These results suggest that the enhancement by calcium hopantenate of the ifenprodil tartrate effect on the vertebral blood flow is due to increased vascular relaxation through the inhibition of Ca2+ influx.

Animals↗
PubMed2004

Demographic and clinical factors associated with development of brimonidine tartrate 0.2%-induced ocular allergy.

PURPOSE: To identify demographic and clinical characteristics associated with the development of brimonidine tartrate 0.2%-induced ocular allergy. PATIENTS AND METHODS: In this retrospective study, 133 patients affected by primary open-angle, pigmentary, narrow angle, or pseudo-exfoliative glaucoma and treated with brimonidine tartrate 0.2% were divided into two groups: allergic and non allergic to brimonidine tartrate 0.2%. The distribution of demographic (age and sex), local (history of allergic conjunctivitis, previous eye-drop ocular allergy, use of other concurrent topical medications, amount of topical medications previously used, use of contact lenses, and tear film production), and systemic (history of systemic allergies and use of systemic drugs) factors was evaluated by comparing the brimonidine tartrate 0.2% allergic and the non-allergic groups. RESULTS: In this study, 13.5% of patients (18 of 133) developed brimonidine ocular allergy generally within two weeks from the beginning of treatment (mean time 14.8 +/- 17.9 days). The brimonidine tartrate 0.2% allergic group showed a significantly higher frequency of history of ocular allergy to eye-drops (P = 0.048) and to topical beta-blockers (P = 0.019) when compared with the brimonidine tartrate 0.2% non-allergic group. Moreover, the allergic group showed a decreased tear film production (P = 0.044). CONCLUSION: This study showed that history of eye-drop allergies and reduction of tear film production were more frequently associated with the development of brimonidine tartrate 0.2%-induced ocular allergy.

Adrenergic alpha-Agonists↗
PubMed2005

Supramolecular structures of 1-phenylethylammonium tartrates.

The structures of six 1-phenylethylammonium tartrates have been determined and in each of them a distinctive hydrogen-bonded anion substructure can be identified. (S)-1-Phenylethylammonium (R,R)-hydrogen tartrate [(I), P21, Z'=1] contains anion sheets built from a single type of R4(4)(22) ring with cations pendent, via three N-H...O hydrogen bonds, from just one face of the sheet. (S)-1-Phenylethylammonium rac-hydrogen tartrate [(II), P21, Z'=2] and its enantiomorph (R)-1-phenylethylammonium rac-hydrogen tartrate [(III), P21, Z'=2] contain anion sheets built from four types of ring, R2(2)(10), R2(2)(12), R2(4)(14) and R4(4)(20), and there are cations pendent from both faces of the sheet. The anion substructure in bis[(S)-1-phenylethylammonium] (R,R)-tartrate [(IV), P2(1), Z'=1] consists of simple C(5) chains, which are linked into sheets by the cations, while in bis(rac-1-phenylethylammonium) (R,R)-tartrate [(V), P2(1), Z'=2] there are anion sheets containing two distinct types of R4(4)(22) ring, with equal numbers of (R) and (S) cations pendent from each face of the anion sheet. Bis[(R)-1-phenylethylammonium] rac-tartrate methanol hemisolvate [(VI), P1, Z'=4, with 14 independent components in the asymmetric unit] contains anion sheets built from two types of R2(2)(12) ring and two types of R6(6)(32) ring; half of the cations and half of the methanol molecules are pendent from each face of the sheet.

Crystallization↗
PubMed2003

Discrimination of d-tartrate-fermenting and -nonfermenting Salmonella enterica subsp. enterica isolates by genotypic and phenotypic methods.

A multiplex PCR and an improved lead acetate test were developed to discriminate d-tartrate-fermenting and -nonfermenting Salmonella enterica subsp. enterica strains. Both methods showed an accuracy of 100% when 125 Salmonella strains belonging to 15 serovars were tested. Special emphasis was given to S. enterica subsp. enterica serovar Paratyphi B isolates because of the clinical importance of its d-tartrate-nonfermenting variant and the recently increasing numbers of cases of human outbreaks caused by its fermenting variant (formerly Salmonella serovar Java). The lead acetate test described previously (G. A. Alfredsson, R. M. Barker, D. C. Old, and J. P. Duguid, J. Hyg. 70:651-666, 1972) was modified in the inoculation and incubation procedure. The PCR assay was based on the genotypic difference of the presence (d-tartrate-fermenting strains) or absence (d-tartrate-nonfermenting strains) of the ATG start codon for the gene STM 3356, which encodes a putative cation transporter. Sequence data revealed a nucleotide exchange from G to A within the ATG start codon of gene STM 3356 in the d-tartrate-nonfermenting strains. In order to increase the reliability of the PCR assay, a positive control based on a Salmonella genus-specific primer set for the detection of Salmonella DNA was included. The PCR-based discrimination needs only several hours compared to 6 days needed by the improved lead acetate test to obtain reliable results. Consequently, the PCR d-tartrate assay should be the method of choice for the discrimination of d-tartrate-fermenting and -nonfermenting Salmonella strains in the future.

Base Sequence↗
PubMed2005

A stability indicating LC method for rivastigmine hydrogen tartrate.

An isocratic, reversed-phase liquid chromatographic (RPLC) method was developed for the quantitative determination of Rivastigmine hydrogen tartrate, a cholinesterase inhibitor in bulk drugs and in pharmaceutical dosage forms. The developed method is also applicable for the related substance determination of Rivastigmine hydrogen tartrate in bulk drugs. The chromatographic separation was achieved on a Waters X Terra RP18 (250 mm x 4.6 mm, 5 microm) column using aqueous 0.01 M sodium-1-heptane sulphonate (pH: 3.0 with dilute phosphoric acid)-acetonitrile (72:28, v/v) as a mobile phase. The chromatographic resolution between Rivastigmine and its potential impurity, namely (S)-3-(1-dimethylaminoethyl) phenol (Imp 1) was found to be greater than four. Forced degradation studies were performed for Rivastigmine hydrogen tartrate bulk drug using acid (0.5 N hydrochloric acid), base (0.5 N sodium hydroxide), oxidation (3% hydrogen peroxide), heat (60 degrees C) and UV light (254 nm). No degradation was observed for Rivastigmine hydrogen tartrate except in base hydrolysis and the formed degradation product was found to be Imp 1. The mass balance of Rivastigmine hydrogen tartrate was close to 100 in all the stress conditions. The limit of detection (LOD) and limit of quantification (LOQ) of Imp 1 were found to be 100 and 300 ng/ml, respectively, for 10 microl injection volume. The percentage recovery of Imp 1 in bulk drug sample was ranged from 95.2 to 104.3. The active pharmaceutical ingredient was extracted from its finished dosage form (capsule) using water. The percentage recovery of Rivastigmine hydrogen tartrate was ranged from 99.2 to 101.3 and 98.6 to 101.5 in bulk and pharmaceutical formulation samples, respectively. Rivastigmine hydrogen tartrate sample solution and mobile phase were found to be stable for at least 48 h. The developed method was validated with respect to linearity, accuracy, precision, robustness and forced degradation studies prove the stability indicating power of the method.

Chromatography, Liquid↗
PubMed2002

A three-layer guar gum matrix tablet for oral controlled delivery of highly soluble metoprolol tartrate.

The objective of the study is to design oral controlled drug delivery systems for highly water-soluble drugs using guar gum as a carrier in the form of a three-layer matrix tablet. Metoprolol tartrate was chosen as a model drug because of its high water solubility. Matrix tablets containing either 30 (M1), 40 (M2) or 50% (M3) of guar gum were prepared by wet granulation technique using starch paste as a binder. Three-layer matrix tablets of metoprolol tartrate were prepared by compressing on both sides of guar gum matrix tablet granules of metoprolol tartrate M1, M2 or M3 with either 50 (TL1M1, TL1M2 or TL1M3) or 75 mg (TL2M1, TL2M2 or TL2M3) of guar gum granules as release retardant layers. Both the matrix and three-layer matrix tablets were evaluated for hardness, thickness, drug content uniformity, and subjected to in vitro drug release studies. The amount of metoprolol tartrate released from the matrix and three-layer matrix tablets at different time intervals was estimated by using a HPLC method. Matrix tablets of metoprolol tartrate were unable to provide the required drug release rate. However, the three-layer guar gum matrix tablets (TL2M3) provided the required release rate on par with the theoretical release rate for metoprolol tartrate formulations meant for twice daily administration. The three-layer guar gum matrix tablet (TL2M3) showed no change either in physical appearance, drug content or in dissolution pattern after storage at 40 degrees C/75% RH for 6 months. The FT-IR study did not show any possibility of metoprolol tartrate/guar gum interaction with the formulation excipients used in the study. The results indicated that guar gum, in the form of three-layer matrix tablets, is a potential carrier in the design of oral controlled drug delivery systems for highly water-soluble drugs such as metoprolol tartrate.

Administration, Oral↗
PubMed2006

An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity.

An isothermal titration calorimetric study of the binding of substrates and inhibitors to different complexes of tartrate dehydrogenase (TDH) from Pseudomonas putida was carried out. TDH catalyzes the nicotinamide adenine dinucleotide (NAD)-dependent oxidative decarboxylation of d-malate and has an absolute requirement for both a divalent and monovalent metal ion for activity. The ligands Mn(2+), meso-tartrate, oxalate, and reduced nicotinamide adenine dinucleotide (NADH) bound to all TDH complexes with a stoichiometry of 1 per enzyme dimer. The exception is NAD, which binds to E/K(+), E/K(+)/Mn(2+), and E/K(+)/Mg(2+) complexes with a stoichiometry of two per enzyme dimer. The binding studies suggest a half-of-the-sites mechanism for TDH. No significant heat changes were observed for d-malate in the presence of the E/K(+)/Mn(2+) complex, suggesting that it did not bind. In contrast, meso-tartrate does bind to E/K(+)/Mn(2+) but gives no significant heat change in the presence of E/Mn(2+), suggesting that K(+) is required for meso-tartrate binding. meso-Tartrate also binds with a large DeltaC(p) value and likely binds via a different binding mode than d-malate, which binds only in the presence of NAD. In contrast to all of the other ligands tested, the binding of Mn(2+) is entropically driven, likely the result of the entropically favored disruption of ordered water molecules coordinated to Mn(2+) in solution that are lost upon binding to the enzyme. Oxalate, a competitive inhibitor of malate, binds with the greatest affinity to E/K(+)/Mn(2+)/NADH, and its binding is associated with the uptake of a proton. Overall, with d-malate as the substrate, data are consistent with a random addition of K(+), Mn(2+), and NAD followed by the ordered addition of d-malate; there is significant synergism in the binding of NAD and K(+). Although the binding of meso-tartrate also requires enzyme-bound K(+) and Mn(2+), the binding of meso-tartrate and NAD is random.

Alcohol Oxidoreductases↗
PubMed2003

Radical mechanisms in the radiosterilization of metoprolol tartrate solutions.

PURPOSE: Study of the radical mechanisms in the radiosterilization of metoprolol tartrate aqueous solutions in order to determine the parameters governing its radiostability. METHODS: Pulse radiolysis with pseudo-first-order kinetics to measure Ihe reaction rate constants of hydrated electrons and hydroxyl radicals with metoprolol tartrate. Chemsimul was used to solve the decay kinetics of transients and to simulate the radiolysis of metoprolol tartrate solutions. RESULTS: Hydrated electrons react with metoprolol and the tartrate ion with rate constants of 6.8 x 10(7) M(-1) s(-1) and 1.7 x 10(7) M(-1) s(-1), respectively. Hydroxyl radicals react with metoprolol and the tartrate ion with rate constants of 5.2 x 10(9) M(-1) s(-1) and 5.5 x 10(8) M(-1) s(-1), respectively. The hydroxyl-metoprolol transients are found to scavenge the superoxide anion (5.5 x 10(10) M(-1) s(-1)), react with oxygen (1.0 x 10(8) M(-1) s(-1)), and follow a biradical decay (2.0 x 10(8) M(-1) s(-1). A simplified radical mechanism is used to simulate the loss of potency of metoprolol tartrate aqueous solutions during radiosterilization. CONCLUSIONS: To decrease the loss of potency of metoprolol tartrate. the sterilization dose must be lowered and very high dose rates used.

Adrenergic beta-Antagonists↗
PubMed1998

Effect of brimonidine tartrate on ocular hemodynamic measurements.

OBJECTIVE: To study the effect of a selective alpha 2-adrenoreceptor agonist, brimonidine tartrate, on ocular hemodynamics. SUBJECTS AND METHODS: Eighteen patients with ocular hypertension were enrolled in a prospective, randomized, double-masked study in which 0.2% brimonidine tartrate, administered twice daily, was compared with its vehicle in a crossover fashion. The effect on the ocular circulation was assessed by color Doppler ultrasound, which measured blood flow velocities (peak systolic and end diastolic velocities) in the central retinal, ophthalmic, nasal, and temporal ciliary arteries. The following tests were performed at 2 weekly intervals on both treatments, 0.2% brimonidine tartrate and the placebo: intraocular pressure, heart rate, blood pressure, and color Doppler ultrasound. RESULTS: Velocities and resistivity indices measured by color Doppler ultrasound in the ophthalmic artery, central retinal artery, nasal artery, and temporal ciliary arteries showed no statistically significant differences between the placebo and 0.2% brimonidine tartrate when compared with baseline values and between the groups. Intraocular pressure was decreased by 17.7% +/- 9.5% with 0.2% brimonidine tartrate (vs 9% +/- 8% with placebo). CONCLUSION: The hemodynamics of the posterior segment of the eye as measured by color Doppler ultrasound do not appear to be altered by 2% brimonidine tartrate.

Adrenergic alpha-Agonists↗
PubMed1989

The effect of tartrate on bone cell acid phosphatase activity: a quantitative cytochemical study.

Tartrate-resistant acid phosphatase activity (TRAPase) is widely used as a cytochemical marker to distinguish osteoclasts from macrophages and other related cell types. The degree of tartrate resistance, however, may depend on which reaction methods, tissues, or species are used. To investigate this further, we have measured the amount of cytochemical reaction product by microdensitometry. We compared osteoclast acid phosphatase (APase) activity in fresh frozen sections of neonatal rat calvaria using two different reaction methods; one is commonly employed for qualitative histochemistry and includes alpha naphthyl phosphate as substrate, simultaneous coupling to the chromagen Fast Garnet, and a 30-minute reaction time (method A). The other may be used to measure enzyme reaction rates in cells in situ and employs conditions suitable for initial velocity kinetics, namely naphthol-ASBI phosphate as substrate, post coupling to Fast Garnet, and a 2-minute reaction time. Although enzyme reaction rates differed greatly between the two methods, significant inhibition of APase activity by tartrate was observed in calvarial osteoclasts (69% and 59% with methods A and B, respectively), osteoblasts, and spleen macrophages. Using method B, mouse calvarial osteoclasts had similar APase activity to that seen in the rat. Tartrate produced little inhibition in these mouse cells, in contrast to the observations made with rat tissue, but murine spleen macrophages were significantly tartrate sensitive (40% inhibition with tartrate). On this basis, conclusions regarding the cell specificity of TRAPase should be treated cautiously.

Acid Phosphatase↗
PubMed1991

Fermentation of L-tartrate by a newly isolated gram-negative glycolytic bacterium.

Enrichments on L-tartrate from a freshwater lake sediment yielded a pure culture of anaerobic bacterium designated strain 16Lt1. The rod-shaped organism was motile, did not form spores, and had a gram-negative wall structure. No cytochromes were detected. The mol % G + C of the DNA was 58. The new strain was microaerotolerant, and grew optimally at 30 degrees C and neutral pH in freshwater medium. A wide range of carbohydrates was fermented, with formate, acetate, ethanol, lactate and succinate being the end-products detected. L-tartrate and citrate were fermented to formate, acetate and CO2. L-tartrate was fermented by the dehydratase pathway, and glucose by the Embden-Meyerhof-Parnas pathway. Fumarate was reduced, but nitrate, sulfate, sulfur and thiosulfate were not used as terminal electron acceptors. Glucose metabolism was constitutive, whereas L-tartrate-degrading activity was inducible. When glucose and L-tartrate were both present as substrates, growth was diauxic with glucose being metabolized first. The growth rate and growth yield were higher on glucose than on L-tartrate. Strain 16Lt1 has been deposited with the Deutsche Sammlung von Mikroorganismen as 'Bacteroides' sp. DSM6268.

Bacteroides↗
PubMed2004

Effect of brimonidine tartrate 0.2% ophthalmic solution on pupil size.

PURPOSE: To evaluate the effect of brimonidine tartrate 0.2% ophthalmic solution on pupil size under scotopic and photopic luminance conditions in persons considering laser refractive surgery. SETTING: Ophthalmic Health Center, Tel Aviv, Israel. METHODS: The pupil size was measured in 36 eyes of 36 participants under scotopic and photopic conditions using the Colvard pupillometer (Oasis Medical) before and after brimonidine tartrate drops were administered. The pupil size was subsequently measured after 30 minutes and 4 and 6 hours. RESULTS: No difference was found in pupil size before brimonidine tartrate instillation in eyes with light or dark irides. Before instillation, the mean photopic pupil size was 4.81 mm +/- 0.54 (SD) (range 4.0 to 6.0 mm). At 30 minutes, all pupils became miotic, with a mean size of 3.77 +/- 0.51 mm (range 3.0 to 5.0 mm) (P<.0001). After 6 hours, 27.8% of the pupils had returned to their previous size. Before brimonidine tartrate administration, the mean scotopic pupil size was 6.22 +/- 0.73 mm (range 5.0 to 8.0 mm). There was significant miosis to 4.57 +/- 0.84 mm (range 3.0 to 6.5 mm) (P<.0001) that continued for at least 6 hours. The miotic effect of brimonidine tartrate was stronger in eyes with light irides. CONCLUSIONS: Brimonidine tartrate caused significant miosis, especially under scotopic conditions, most likely from its alpha-2 adrenergic effect. Under photopic luminance conditions, the miotic effect was pronounced.

Adrenergic alpha-Agonists↗
PubMed2000

Aluminum speciation studies in biological fluids. Part 6. Quantitative investigation of aluminum(III)-tartrate complex equilibria and their potential implications for aluminum metabolism and toxicity.

Recent epidemiological studies have confirmed the existence of a correlation between aluminum level in low-silica drinking water and prevalence of Alzheimer's disease. Also, oral aluminum-based phosphate binders and antacids may induce acute aluminum toxicity. Whatever the source of the metal ingested, its bioavailability is a function of the chemical forms under which it occurs in the gastrointestinal tract, i.e. of the ligands with which the Al3+ ion may associate. Dietary acids in particular can favor the bioavailability of aluminum in different ways: by increasing its solubility, by complexing it into neutral species, and/or by acting indirectly on its absorption process. Among these, tartaric acid is commonly found in fruits and in industrial foods and drinks, and may therefore be ingested together with environmental or/and therapeutic aluminum. The present work examines its potential influence on aluminum bioavailability. Firstly, Al(III)-tartrate complex formation constants have been determined under physiological conditions (37 degrees C, 0.15 M NaCl). Then these constants have been used to simulate the influence of tartrate on aluminum speciation in different gastrointestinal situations in which phosphate was also taken into account. Under normal conditions of aluminum contamination, tartrate is expected to keep the metal soluble throughout the whole pH range of the small intestine, which is likely to enhance its bioavailability. Even at low concentrations, tartrate also gives rise to two neutral complexes that span over the 1.5-7.5 pH interval, a phenomenon that is aggravated by increased aluminum levels as may result from aluminum hydroxide therapy. The co-occurrence of dietary phosphate reduces the fraction of aluminum neutralized by tartrate under normal conditions, but this effect quickly decreases with increasing aluminum doses. Even the therapeutic use of aluminum phosphate is not expected to be totally safe in the presence of tartaric acid. As plasma simulations show that no aluminum mobilization can be expected from tartrate that could enhance aluminum excretion, avoiding ingestion of tartaric acid during any form of aluminum-based therapy appears advisable.

Aluminum↗
PubMed1998

Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.

Acid phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic acid phosphatase level. Human prostatic acid phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic acid phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic acid phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic acid phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.

Acid Phosphatase↗
PubMed1993

Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the class I fumarase genes.

The genes encoding an oxygen-labile stereospecific L-tartrate dehydratase (L-Ttd, EC 4.2.1.32) have been identified as the orfZ1 and orfZ2 genes located upstream of the rpsU-dnaG-rpoD operon at 67 min in the Escherichia coli linkage map. They were previously cloned and sequenced by M. Nesin and others (Gene 51, 149-161, 1987) and have now been independently cloned, partially resequenced, and designated as an operon (ttdAB) containing two translationally coupled genes. The enzyme behaves as a tetramer (M(r) 105,000) containing two pairs of non-identical subunits, TtdA (M(r) 32589) and TtdB (M(r) 22641), which otherwise resembles the homodimeric iron-sulphur-containing Class I fumarases of E. coli and Bacillus stearothermophilus. The amino acid sequences of the TtdA-TtdB subunits are colinearly related to a single fumarase subunit, indicating a common evolutionary ancestry. E. coli can use L-, D- and meso-tartrates as aerobic growth substrates and as reducible substrates for supporting anaerobic growth on glycerol. L-Ttd was induced during anaerobic growth on glycerol plus L- and meso-tartrates, and a stereospecific D-tartrate dehydratase was induced by all three stereoisomers under comparable conditions. No meso-tartrate dehydratase was detected, nor were any dehydratases detected after aerobic growth on tartrate minimal media suggesting that different catabolic routes operate under aerobic conditions.

Amino Acid Sequence↗
PubMed1986

Demonstration of tartrate-resistant acid phosphatase in un-decalcified, glycolmethacrylate-embedded mouse bone: a possible marker for (pre)osteoclast identification.

Fixed, undecalcified mouse long bones were embedded in glycol methacrylate (GMA), sectioned, and incubated for acid phosphatase in the presence or absence of tartrate, to investigate the feasibility of tartrate-resistant acid phosphatase as a histochemical marker for osteoclast identification. Naphthol AS-BI phosphate was used as the substrate and hexazonium pararosanaline as coupler. Cytocentrifuge preparations of mouse, rat, and quail bone marrow or frozen and GMA sections of mouse splenic tissue were used as controls to specify acid phosphatase activity. After adequate fixation, acid phosphatase activity sensitive to tartrate inhibition (TS-AP) was demonstrated in macrophages from spleen, bone marrow, and loose connective tissue surrounding bone rudiments. Acid phosphatase activity resistant to tartrate inhibition (TR-AP), was detected in multi-nuclear osteoclasts and in some mononuclear cells from bone marrow and periosteum. In cytocentrifuge preparations and frozen sections of mouse spleen, TR-AP was demonstrated after simultaneous incubation with substrate and tartrate. In GMA sections, however, TR-AP could only be demonstrated after pre-incubation with tartrate before application of substrate. We suggest that histochemical demonstration of TR-AP versus TS-AP on GMA-embedded bone sections by means of a pre-incubation method can be used as an identification marker of (pre)osteoclasts. Plastic embedding is recommended for its excellent preservation of morphology and enzyme activity.

Acid Phosphatase↗
PubMed2002

Effects of meluadrine tartrate and ritodrine hydrochloride on oxytocin-induced uterine contraction, uterine arterial blood flow and maternal cardiovascular function in pregnant goats.

This study was designed to elucidate the effects of meluadrine tartrate on oxytocin-induced uterine contraction and maternal hemodynamics in unanesthetized, chronically instrumented pregnant goats. After the administration of meluadrine tartrate or ritodrine hydrochloride to pregnant goats, changes in heart rate (HR), arterial blood pressure (AOP), and arterial blood pH and gasses (P(O2) and P(CO2)) in the mother, as well as changes in intrauterine pressure (IUP) and uterine arterial blood flow (UBF), were measured. The escalating administration of meluadrine tartrate (0.03, 0.1, 0.3 and 1 micro g. kg(-)(1). min(-)(1)) or ritodrine hydrochloride (1, 3, 10 and 30 microg. kg(-)(1). min(-)(1)) to the maternal femoral vein caused a marked and similar inhibition in oxytocin-induced uterine contraction (a rise in IUP). By these escalating dosings, maternal HR was increased dose-dependently in both treatment groups; however, the degree of the HR increase in the meluadrine tartrate-treatment group was significantly less than that in the ritodrine hydrochloride-treatment group. Furthermore, the degree of the UBF decrease in the meluadrine tartrate-treatment group was significantly less than that in the ritodrine hydrochloride-treatment group. The present study suggests that meluadrine tartrate has a mild influence on the maternal cardiovascular function relative to the effects of ritodrine taking the potent efficacy on oxytocin-induced uterine contraction into account.

Adrenergic beta-Agonists↗