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PubMed1992

Cardiovascular effects of R- and S-enantiomers of Ro 22-9194, (2R)-2-amino-N- (2,6-dimethylphenyl)-N-[3-(3-pyridyl)propyl]propionamide D-tartrate and (2S)-2-amino-N-(2,6-dimethylphenyl)-N-[3-(3-pyridyl)propyl]propionamide L-tartrate, in dog heart preparations.

A newly synthesized compound, Ro 22-9194, relates in part of to the chemical structure of lidocaine. The cardiac effects of R- and S-enantiomers of Ro 22-9194 were investigated on isolated right atrial and left ventricular (LV) preparations which were cross-perfused with blood from another donor dog and an anesthetized open-chest dog. Each enantiomer (1-1,000 micrograms) decreased dose-dependently the sinus rate and atrial developed tension in the isolated right atrium (RA). The negative chronotropic responses to R- and S-enantiomers were not significantly different, and the negative inotropic responses to R- and S-enantiomers were also generally comparable. Both R- and S-enantiomers (10-3,000 micrograms) also decreased the ventricular developed tension in a dose-related manner similarly. In neurally decentralized, anesthetized, open-chest dogs, R- and S-enantiomers (0.1-3 mg/kg) injected into the femoral vein dose-dependently prolonged atrioventricular (A-V) conduction time and decreased heart rate (HR) and arterial blood pressure (ABP). Each enantiomer (3 mg/kg intravenously, i.v.) prolonged the interval between His bundle and ventricle rather than the interval between atrium and His bundle. There was no significant difference between R- and S-enantiomer-induced negative dromotropic actions. The duration of the negative dromotropic response to each enantiomer (3 mg/kg i.v.) was longer than that of the decrease in BP. These results suggest that the negative chronotropic, inotropic, and dromotropic effects of R- and S-enantiomers of Ro 22-9194 are not stereospecific in dog heart.

Analysis of Variance↗
PubMed1988

[The stability of norepinephrine hydrogen tartrate, epinephrine hydrogen tartrate and isoprenaline sulfate. 29. The stability of drugs and preparations].

Stability testing of derivatives of brenzcatechine [norepinephrine hydrogentartrate (1), epinephrine hydrogentartrate (2), isoprenaline sulfate (3)] was carried out by stress investigation storing them at different temperatures. Substances of different charges which had been stored under normal conditions were analyzed. After a period of induction all three substances had been decomposed with a higher velocity. The order of kinetic process could not be determined. The storage life time was calculated by the aid of nonlinear regression. Time limit for storage of 5 years for 1 and 2 were confirmed. We suggest to extend it for 3 to 10 years.

Drug Stability↗
PubMed1995

Sequence and mutational analysis of a tartrate utilization operon from Agrobacterium vitis.

The grapevine is the natural host of the tumorigenic bacterium Agrobacterium vitis. Most of the A. vitis isolates can use tartrate, an unusually abundant compound in grapevine. The nopaline strain, AB4, contains a 170-kb conjugative plasmid (pTrAB4) encoding tartrate utilization. A 5.65-kb pTrAB4 region which enables non-tartrate-utilizing Agrobacterium tumefaciens to grow on tartrate was sequenced and mutagenized with the transcriptional fusion transposon Tn5-uidA1. This DNA fragment contains four intact open reading frames (ORFs) (ttuABCD) required for tartrate-dependent growth. The mutant phenotypes of each ORF, their homologies to published sequences, and their induction patterns allowed us to propose a model for tartrate utilization in A. vitis. ttuA encodes a LysR-like transcriptional activator and is transcribed in the absence of tartrate. ttuB codes for a protein with homology to transporter proteins and is required for entry of tartrate into bacteria. ttuC codes for a tartrate dehydrogenase, while ttuD lacks homology to known sequences; the growth properties of ttuD mutants suggest that TtuD catalyzes the second step in tartrate degradation. A fifth incomplete ORF (ttuE) encodes a pyruvate kinase which is induced by tartrate and required for optimal growth. Although the ttuABCD fragment allows growth of A. tumefaciens on tartrate, it does not provide full tartrate utilization in the original A. vitis background.

Amino Acid Sequence↗
PubMed1985

[Inhibitory mechanism of ifenprodil tartrate on rabbit platelet aggregation].

The effects of dl-erythro-4-benzyl-alpha-(4-hydroxyphenyl)-beta-methyl-l-piperidine-eth anol tartrate (ifenprodil tartrate) on rabbit platelet aggregation in vitro and ex vivo were studied. Ifenprodil tartrate inhibited platelet aggregation in vitro induced by ADP, collagen and epinephrine. It also inhibited 5-hydroxytryptamine (5-HT) uptake into platelets and 5-HT release from platelets. Since these inhibitory effects of ifenprodil tartrate on the functions of rabbit platelets were similar to the effects of imipramine, the effects of ifenprodil tartrate may be due to the stabilizing action of ifenprodil tartrate on the platelet membrane. The platelet aggregation by ADP was significantly inhibited in rabbits after oral administration of ifenprodil tartrate, the maximal plasma level of ifenprodil being reached at 20 ng/ml ex vivo, while the maximal level was only 1/40 of the minimal concentration of ifenprodil tartrate necessary to inhibit platelet aggregation in vitro. These results indicate that factors other than ifenprodil tartrate acting directly on the platelets (e.g., PGI2 which is an endogenous inhibitor of platelet aggregation) are involved in inducing the inhibitory effects of ifenprodil tartrate on platelet aggregation ex vivo. The effects of ifenprodil tartrate on both PGI2 release from the aorta and the inhibitory effects of PGI2 on platelet aggregation in vitro were investigated: PGI2 was found to intensify the inhibitory effects of ifenprodil tartrate on platelet aggregation in vitro, but there was little effect, if any, on PGI2 release. Therefore, it is considered that the ex vivo effects of ifenprodil tartrate might be due to its interaction with endogenous PGI2 in the blood.

Animals↗
PubMed1980

Physiological basis for meso-tartrate sensitivity in some strains of Salmonella typhimurium.

meso-Tartrate inhibited the growth of non-meso-tartrate-utilizing strains of Salmonella typhimurium in peptone water media and mineral salts media with some, but not all, carbon sources. C-R intermediates of the tricarboxylic acid cycle or compounds readily converted to them and substrates metabolized independently of the C-6 part of the cycle spared bacteria from the inhibitory effects of meso-tartrate when added to cultures along with meso-tartrate. Experiments with cell-free extracts of non-meso-tartrate-utilizing strains from batch and continuous cultures showed that meso-tartrate was a competitive inhibitor of isocitrate dehydrogenase and isocitrate lyase activities and also inhibited citrate synthase and malate synthase activities. The synthesis of these enzymes was not inhibited by meso-tartrate. The isocitrate enzymes of meso-tartrate-utilizing strains of S. typhimurium were similarly inhibited by meso-tartrate, but inhibition of the growth of meso-tartrate-utilizing strains was demonstrable only in uninduced cultures in which the intracellular concentrations of meso-tartrate were high.

Citrate (si)-Synthase↗
PubMed1995

Vinorelbine tartrate and paclitaxel combinations: enhanced activity against in vivo P388 murine leukemia cells.

BACKGROUND: Many critical cellular functions such as mitosis, cell movement, and maintenance of cell structure are performed by microtubules. Antimicrotubule agents (which disrupt or block the formation of microtubules) are among the most widely used anticancer drugs and have contributed to the curative therapy of many neoplasms. Recently, two new antimicrotubule agents, vinorelbine tartrate (Navelbine) and paclitaxel (Taxol) have demonstrated clinical activity against ovarian, breast, and non-small-cell lung carcinomas. These agents target microtubules at different sites, and they both interfere with mitotic spindle function. Since vinorelbine tartrate and paclitaxel have shown a similar antitumor profile in clinical trials thus far, it is reasonable to expect that they may be used interchangeably in some combination therapies or perhaps with each other in the same treatment regimen. PURPOSE: On the basis of their similar activity profile in clinical trials, we decided to investigate the therapeutic outcome of a vinorelbine tartrate and paclitaxel binary drug combination, even though they appeared to have overlapping toxic effects. We wanted to ascertain the effect of this binary drug combination, in an in vivo setting, as it related to host toxicity and antitumor activity. METHODS: CDF-1 female mice that were implanted intraperitoneally with one million P388 murine leukemia cells were treated intraperitoneally with vinorelbine tartrate, paclitaxel, or a combination of the two drugs on a day-1, -5, and -9 dosing schedule. Experimental groups had between five and eight mice per group. Vinorelbine tartrate was administered at either 8, 12, 16, 20, or 24 mg/kg and paclitaxel at either 4.5, 18, or 36 mg/kg. RESULTS: As single agents, neither vinorelbine tartrate nor paclitaxel generated meaningful numbers of 60-day cures (i.e., tumor free at day 60). In contrast, optimal combination regimens produced 60-day cures in more than 80% of the mice. The LD10 (dose lethal to 10% of the mice) of vinorelbine tartrate increased approximately 2.5-fold in the presence of paclitaxel and allowed otherwise lethal vinorelbine tartrate doses to be administered safely, which may have contributed to the antitumor efficacy of the combinations. The effect of the time delay between vinorelbine tartrate and paclitaxel administration on toxicity and cures appeared to be contingent on the vinorelbine tartrate dose. CONCLUSIONS: Results suggest that the overlapping toxic effects of vinorelbine tartrate and paclitaxel might not be a deterrent to their use in combination drug therapy. When used appropriately, rather than having enhanced toxic effects, otherwise toxic doses were better tolerated and survival improved over single-agent therapy.

Animals↗
PubMed1983

Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y.

A bifunctional enzyme, L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) (EC 1.1.1.93 and EC 1.1.1. . . , respectively), was discovered in cells of Rhodopseudomonas sphaeroides Y, which accounts for the ability of this organism to grow on L-(+)-malate. The enzyme was purified 110-fold to homogeneity with a yield of 51%. During the course of purification, including ion-exchange chromatography and preparative gel electrophoresis, both enzyme activities appeared to be in association. The ratio of their activities remained almost constant [1:10, L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating)] throughout all steps of purification. Analysis by polyacrylamide gel electrophoresis revealed the presence of a single protein band, the position of which was coincident with both L-(+)-tartrate dehydrogenase and D-(+)-malate dehydrogenase (decarboxylating) activities. The apparent molecular weight of the enzyme was determined to be 158,000 by gel filtration and 162,000 by ultracentrifugation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single polypeptide chain with an estimated molecular weight of 38,500, indicating that the enzyme consisted of four subunits of identical size. The isoelectric point of the enzyme was between pH 5.0 and 5.2. The enzyme catalyzed the NAD-linked oxidation of L-(+)-tartrate as well as the oxidative decarboxylation of D-(+)-malate. For both reactions, the optimal pH was in a range from 8.4 to 9.0. The activation energy of the reaction (delta Ho) was 71.8 kJ/mol for L-(+)-tartrate and 54.6 kJ/mol for D-(+)-malate. NAD was required as a cosubstrate, and optimal activity depended on the presence of both Mn2+ and NH4+ ions. The reactions followed Michaelis-Menten kinetics, and the apparent Km values of the individual reactants were determined to be: L-(+)-tartrate, 2.3 X 10(-3) M; NAD, 2.8 X 10(-4) M; and Mn2+, 1.6 X 10(-5) M with respect to L-(+)-tartrate; and D-(+)-malate, 1.7 X 10(-4) M; NAD, 1.3 X 10(-4); and Mn2+, 1.6 X 10(-5) M with respect to D-(+)-malate. Of a variety of compounds tested, only meso-tartrate, oxaloacetate, and dihydroxyfumarate were effective inhibitors. meso-Tartrate and oxaloacetate caused competitive inhibition, whereas dihydroxyfumarate caused noncompetitive inhibition. The Ki values determined for the inhibitors were, in the above sequence, 1.0, 0.014, and 0.06 mM with respect to L-(+)-tartrate and 0.28, 0.012, and 0.027 mM with respect to D-(+)-malate.

Alcohol Oxidoreductases↗
PubMed1995

Controlled efficacy study of the bioequivalence of Strongid C and generic pyrantel tartrate in horses.

The bioequivalence of Strongid C and generic pyrantel tartrate was determined in a controlled study using 30 horses with naturally acquired endoparasitic infections. Three horses were randomly allocated to each of ten replicates based on quantitative nematode and ascarid egg counts and fecal larvae culture results. Horses within each replicate were randomly assigned to one of three treatment groups. Horses in Treatment Group 1 received only oats; horses in Treatment Group 2 received generic pyrantel tartrate pellets (2.65 mg pyrantel tartrate kg-1) mixed with oats; horses in Treatment Group 3 were fed Strongid C pellets (2.65 mg pyrantel tartrate kg-1) mixed with oats. Horses were treated daily for a 30 day continuous treatment period. At the termination of the study the horses were necropsied and endoparasites recovered, identified, and enumerated. In all instances, no significant difference (P > 0.05) in mean numbers of parasites recovered existed between horses treated with generic pyrantel tartrate and Strongid C. Numbers of gastrointestinal parasites recovered from horses treated with generic pyrantel tartrate or Strongid C were shown to be significantly different (P < 0.05) from numbers of gastrointestinal parasites recovered from non-treated controls for the large strongyles (Strongylus vulgaris, S. edentatus, and Triodontophorus spp.), small strongyles (Cyathostomum spp., Cylicocyclus spp., and Cylicostephanus spp.) and fourth-stage Parascaris equorum. Numbers of adult P. equorum recovered from horses treated with Strongid C were also significantly different (P < 0.05) from those from non-treated controls. Numbers of adult P. equorum recovered from horses treated with generic pyrantel tartrate were not significantly different (P = 0.0761) from those from non-treated controls. The determination of bioequivalence was based upon the 95% confidence interval of the difference between the mean number of parasites recovered from horses treated with generic pyrantel tartrate and the mean number of parasites recovered from horses treated with Strongid C. For all instances in which the numbers of parasites recovered from horses treated with either Strongid C or generic pyrantel tartrate were significantly different from the numbers of parasites recovered from non-treated controls, bioequivalence was demonstrated.

Animal Husbandry↗
PubMed1982

Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function.

Organ cultures of newborn mouse calvaria were used to test the hypothesis that tartrate-resistant acid phosphatase might serve as a biochemical marker for osteoclast function. When bone resorption was stimulated in vitro with either parathyroid hormone or 1,25(OH)2D3, there was a significant increase in both tartrate-resistant and tartrate-sensitivity acid phosphatase activity in the medium relative to cultured controls. Tartrate-resistant activity was localized histochemically primarily over the osteoclast and appeared as three distinct activity bands when electrophoresed on polyacrylamide gels. The tartrate-sensitive activity was found primarily associated with bone cells other than the osteoclast using histochemical techniques, and was resolved into five bands on polyacrylamide gels. The results obtained from biochemical assays, histochemical observations, and polyacrylamide gel electrophoresis suggest that bone resorption in vitro results in the release of tartrate-resistant acid phosphatase from osteoclasts and tartrate-sensitive acid phosphatase from other bone cells as well as osteoclasts. Tartrate-resistant acid phosphatases of bone may be suitable biochemical probes for osteoclasts function, but it will be necessary to achieve further purification in order to develop analytical methods with sufficient sensitivity and specificity (e.g., immunochemical) to ensure precise localization and quantitation.

Acid Phosphatase↗
PubMed2002

Can a determination of tartrate-resistant acid phosphatase predict postmenopausal loss of bone mass?

BACKGROUND: A study was carried out over a 24-month interval to determine if an initial measurement of serum tartrate-resistant acid phosphatase would be predictive of bone mass loss quantified by dual-energy X-ray absorptiometry, as total bone mineral content and total bone mineral content corrected for weight. DESIGN: Sixty-two women were studied (at onset: mean age 59.7 +/- 8.9 years, 10.8 +/- 8.8 years since menopause; at conclusion: mean age 61.9 +/- 8.8 and 13.0 +/- 8.7 since menopause). RESULTS: A paired Wilcoxon test showed a small, but significant, increase in weight (P < 0.05) and decrease in height (P < 0.05). Total bone mineral content and total bone mineral content corrected for weight decreased (P < 0.005 and 0.0001, respectively). Serum tartrate-resistant acid phosphatase increased (P < 0.005). Single-regression analysis showed that the per cent bone mass loss observed between the first and second body bone mineral content measurements correlated negatively with the first serum tartrate-resistant acid phosphatase determination (r = -0.62, P < 0.0001). Changes in tartrate-resistant acid phosphatase correlated negatively with changes in total bone mineral content (r = -0.79, P < 0.0001). In a multiple regression analysis of per cent change in bone mass against initially important variables such as age, years since menopause, weight, and tartrate-resistant acid phosphatase, only tartrate-resistant acid phosphatase was significant (P < 0.0001). The sensitivity and specifity of tartrate-resistant acid phosphatase for evaluating bone loss were 86% and 78%, respectively, and the area under the curve was of 0.83 (95% CI 0.71-0.95). CONCLUSION: These results show that a simple measurement of serum tartrate-resistant acid phosphatase can help to predict the potential rate of bone mass loss in women.

Absorptiometry, Photon↗
PubMed1994

Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.

The gene encoding tartrate dehydrogenase has been cloned from Pseudomonas putida and sequenced. The gene is 1098 nucleotides long and encodes a protein 365 amino acids in length with a calculated M(r) of 40,636. The gene and the protein encoded by it show strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase. Thus, tartrate dehydrogenase is the third member to be identified of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases which have an evolutionarily distinct NAD(+)-binding domain. The poor catalytic properties of tartrate dehydrogenase suggest that it has not been under strong selective pressure to maximize its ability to turn over (+)-tartrate for very long; the homology with isopropylmalate dehydrogenase makes it an attractive candidate for a recent progenitor of tartrate dehydrogenase. beta-Isopropylmalate is a substrate for tartrate dehydrogenase with a Km of 14 +/- 2 microM; it is turned over with a Vmax that is 35% of Vmax in the (+)-tartrate reaction. The gene encoding tartrate dehydrogenase has been expressed in Escherichia coli and large quantities of soluble enzyme can be obtained.

Alcohol Oxidoreductases↗
PubMed1997

A dose-ranging pharmacokinetic study of nicotine tartrate following single-dose delayed-release oral and intravenous administration.

BACKGROUND: Ulcerative colitis is predominantly a disease of non-smokers, and transdermal nicotine is therapeutic but often results in side-effects. Administration of nicotine tartrate as a liquid enema decreases systemic nicotine absorption and may be effective for treatment of active distal ulcerative colitis. Ileocolonic delivery of nicotine tartrate via a delayed release oral capsule would be the preferred route to deliver nicotine to the colon. AIM: To determine the bioavailability and pharmacokinetic parameters of delayed-release oral nicotine tartrate capsules (Eudragit S100 coated) at doses of 3 mg and 6 mg nicotine. METHODS: Twenty healthy human subjects received delayed-release oral nicotine tartrate at one of two doses (each group n = 10): 3 mg and 6 mg nicotine. All subjects also received intravenous nicotine tartrate (at a dose of 15 micrograms nicotine base/kg) during a separate study period. Serum nicotine concentrations were determined by gas chromatography-mass spectrometry. In addition, concentrations of serum cotinine (major nicotine metabolite) were determined by high-performance liquid chromatography in all samples for two subjects (both given 6 mg nicotine). Adverse reactions were determined by questionnaire. RESULTS: The mean bioavailabilities of nicotine after ileocolonic nicotine tartrate administration via delayed-release oral capsules at doses 3 mg and 6 mg nicotine were 41% and 42%, respectively. The ratios (after adjusting for nicotine dose) of cotinine area under the curve (AUC) for delayed-release oral nicotine to cotinine AUC for intravenous nicotine were 1.5 and 1.6 for the two subjects undergoing cotinine pharmacokinetics, demonstrating significant first-pass metabolism. Serum nicotine concentrations did not predict adverse reactions. CONCLUSIONS: Nicotine tartrate delivered to the ileocolon as a delayed-release oral capsule at doses of 3 mg and 6 mg nicotine considerably reduced systemic nicotine bioavailability. This reduction in bioavailability appears to be a result of first-pass hepatic metabolism rather than poor mucosal absorption of nicotine. The therapeutic potential of an ileocolonic delivery formulation of nicotine tartrate, which can potentially limit toxicity by local delivery of high doses of nicotine, should be investigated in patients with ulcerative colitis.

Administration, Oral↗