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At least 19 recordsLinked to original sources

PubMed1982

D-(--)-tartrate dehydratase of Rhodopseudomonas sphaeroides: purification, characterization, and application to enzymatic determination of D-(--)-tartrate.

An isolate of Rhodopseudomonas sphaeroides was capable of growing phototrophically and chemotrophically (mu = 0.15 h(-1) for either condition) with d-(-)-tartrate as the carbon source. A d-(-)-tartrate dehydratase, (d-(-)-tartrate hydrolyase, EC 4.1.2.70) was induced in the presence of d-(-)-tartrate. The enzyme was purified 30-fold from cell extracts of R. sphaeroides to a specific activity of 7.5 U/mg of protein and was subsequently crystallized in the presence of 1 M KCl. The enzyme was homogeneous upon analytical electrophoresis in 5% polyacrylamide gels and by criteria of ultracentrifugation. The native enzyme had a molecular weight of 158,000 +/- 1,000 as determined by gel filtration and ultracentrifugation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single polypeptide chain with an estimated molecular weight of 39,500 +/- 500, indicating that d-(-)-tartrate dehydratase was a tetramer. The isoelectric point of the native enzyme was at pH 5.5. The enzyme catalyzed irreversibly the conversion of d-(-)-tartrate to oxaloacetate and water, and the turnover number was calculated to be 1,185. The reaction followed Michaelis-Menten kinetics, and a K(m) value of 1.8 x 10(-4) M was determined. d-(-)-Tartrate dehydratase required Mg(2+) for activity. The pH optimum was within a range from 6.2 to 7.2, and the activation energy of the reaction (Delta H(0)) was 63.2 kJ/mol. The enzyme was specific for d-(-)-tartrate; it did not react with l-(+)-tartrate, meso-tartrate, and other hydroxycarboxylic acids. d-(-)-Tartrate dehydratase was strongly inhibited by meso-tartrate (50% at 0.6 mM). l-(+)-Tartrate and a variety of hydroxycarboxylic acids caused 50% inhibition at concentrations of >30 mM.

Cations, Divalent↗

PubMed2006

The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli.

Escherichia coli ferments L-tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for L-tartrate uptake and succinate export and its relation to the general C(4)-dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE) gene, is required for the uptake of L-tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the L-tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA, ttdB, and ttdT are cotranscribed. Deletion of ttdT abolished growth by L-tartrate and degradation of L-tartrate completely. Bacteria containing TtdT catalyze L-tartrate or succinate uptake and specific heterologous L-tartrate/succinate antiporting. D-Tartrate is not a substrate for TtdT. TtdT operates preferentially in the direction of tartrate uptake and succinate excretion. The Dcu carriers do not support anaerobic growth on L-tartrate or L-tartrate transport. TtdT is related in sequence and function to CitT, which catalyzes heterologous citrate/succinate antiporting in citrate fermentation.

Bacterial Proteins↗

PubMed1983

Competitive growth experiments with related pairs of tartrate-fermenting and tartrate-non-fermenting strains of Salmonella typhimurium: relevance to biotyping studies.

For each of the isomers of tartaric acid, meso- or d- or l-, a pair of strains of Salmonella typhimurium was obtained, the one, a naturally occurring, non-fermenting strain and the other a spontaneous, tartrate-fermenting mutant derived from it. For each of the pairs of strains, competitive mixed cultures were grown from inocula of the tartrate-fermenting and tartrate-non-fermenting strains in peptone medium without or with the appropriate tartrate isomer. In each experiment, small numbers of tartrate-fermenting bacteria outgrew small or large numbers of tartrate-non-fermenting bacteria in 24 hours in tartrate-containing but not in tartrate-free peptone medium. The results of the experiments are discussed with reference to the choice of the definitive time of reading for tartrate-utilisation tests in the biotyping of S. typhimurium.

Animals↗

PubMed2000

[Tartrate-sensitive and tartrate-resistant acid phosphatases in Amoeba proteus].

In free-living Amoeba proteus (strain B), acid phosphatase (AcP) was examined by disc-electrophoresis in polyacrylamide gel. The tartrate-sensitive amebian AcP was greatly inhibited by dithiothreitol and Cu2+, and only partly inhibited by sodium orthovanadate, ammonium molybdate, EDTA, disodium salt and Mg2+, Ca2+, Zn2+ and Mn2+. On the contrary, it appeared to be resistant to sulfhydryl reagents--4(hydroxymercury) benzoic acid, sodium salt and N-ethylmaleimide. Unlike the tartrate-sensitive enzyme, the tartrate-resistant AcP was greatly inhibited by EDTA and partly inhibited by dithiothreitol, Mg2+ and Cu2+ (Mn2+ > Cu2+), being activated by orthovanadate, molybdate, sulfhydryl reagents, Mg2+, Ca2+ and Zn2+. Both tartrate-sensitive and tartrate-resistant AcPs lack apparently free SH-groups necessary for their catalytic activities. Using 2-naphthyl phosphate as a substrate at pH 4.5, six AcP electromorphs were revealed in cytosol and sediment, four of these being most frequently localized in the former, and two in the latter. Two other AcP electromorphs were confined to the sediment only. Depending on the quantity of sedimented amoebae making a homogenate (0.5 or 2.0 cm3), that was added to Percoll solution, the lysosomal AcP fraction in polyacrylamide gel was represented by one or two tartrate-sensitive electromorphs. Therefore, tartrate-resistant AcP in A. proteus may be a lysosomal enzyme, while tartrate-resistant AcP may correspond to serine/threonine protein phosphatase.

Acid Phosphatase↗

PubMed1983

Adaptation of Rhodopseudomonas sphaeroides to Growth on d-(-)-Tartrate and Large-Scale Production of a Constitutive d-(-)-Tartrate Dehydratase During Growth on dl-Malate.

Of 10 strains of the purple non-sulfur bacterium Rhodopseudomonas sphaeroides, 8 acquired the ability to grow on d-(-)-tartrate; however, growth occurred only after extended lag phases ranging from 2 to 14 days. These lag phases occurred because only a small number of inoculum cells were able to grow by forming the enzyme d-(-)-tartrate dehydratase [d-(-)-tartrate hydro-lyase; EC number not yet available]. Once cells had grown on d-(-)-tartrate, d-(-)-tartrate dehydratase was formed constitutively. Therefore, mass cultivation of R. sphaeroides for production of large quantities of enzyme was possible on substrates much cheaper than d-(-)-tartrate. When 0.38 mol of dl-malate was used as a substrate in a chemotrophic fed-batch culture, a final biomass of 15 g (dry weight) liter and 1,500 U of d-(-)-tartrate dehydratase liter of culture were formed. The enzyme can be used for selective cleavage of racemic tartaric acid and for quantitative determination of d-(-)-tartrate.

Journal Article↗

PubMedDate not supplied

A study of factors affecting the labelling of tartrate with 188Re and the transchelation of the 188Re from the tartrate to a protein.

The formation of 188Re-tartrate for use in transchelation reactions and the transchelation of the 188Re onto albumin was studied. Two labelled tartrate products were separated using a non-traditional mobile phase on ITLC strips. Tartrate labelling yield increases with pH but so does the instability when the product is exposed to air. Lower pH's are preferred when oxygen-free labelling conditions can be achieved. Higher tin levels protect against air oxidation. Stability of the Re-tartrate complex is supported by addition of ascorbic acid and ferrous sulphate, however both these agents decreased the rate of the formation of the Re-tartrate complex. The labelling efficiency of a perrhenate solution decreased with the time for which it is stored prior to the labelling reaction, depending on the radioactive concentration.Re-albumin transchelation efficiency increases with the tartrate concentration, while increased stability of the Re-tartrate complex lowers the transchelation yields of Re-albumin.

Chelating Agents↗

PubMed2001

Crystal structure analysis and chiral recognition study of Delta-[Ru(bpy)2(py)2][(+)-O,O'-dibenzoylD-tartrate].12H2O and Lambda-[Ru(bpy)2(py)2][(-)-O,O'-dibenzoyl-L-tartrate].12H2O.

The molecular structure and crystal-packing mode of the enantiopure chiral building blocks Delta-[Ru(bpy)(2)(py)(2)][(+)-O,O'-dibenzoyl-D-tartrate].12H(2)O (I) and Lambda-[Ru(bpy)(2)(py)(2)][(-)-O,O'-dibenzoyl-L-tartrate].12H(2)O (II) have been determined by single-crystal X-ray diffraction data. This study proposes a model of how the L- and D-dibenzoyltartrate anions recognize the chirality of the hydrophobic [Ru(bpy)(2)(py)(2)](2+) complex. The monoclinic unit cell contains four complex cations, four tartrate anions, and 48 water molecules. Since there are no possibilities to form hydrogen bonds between the cations and anions, chiral recognition is due to crystal packing. Two benzoyl rings of two different tartrate anions are gripping the two bpy-planes of the Ru-complex. Further a third benzoyl ring from a tartrate anion is packed between the two pyridine rings, favoring one enantiomeric form to crystallize from aqueous solution. Crystal structure data for I at 153 K: a = 15.342(3) A, b = 19.200(4) A, c = 18.872(4) A, beta = 104.841(3) degrees, monoclinic space group C(2), R(1)= 0.0239 (I > 2sigma(I)), R(2) = 0.0606, Flack parameter = 0.0115 (with esd 0.0166). For II at 293 K: a = 15.376(4) A, b = 19.388(11) A, c = 19.085(7) A, beta = 105.11(2) degrees, monoclinic space group C121, R(1)= 0.0686 (I > 2sigma(I)), R(2) = 0.1819, Flack parameter = -0.0100 (with esd 0.0521).

Journal Article↗

PubMed1988

Total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum: biological variations and reference limits.

We studied several factors affecting biological variation in serum acid phosphatases in a population of 1195 apparently healthy subjects four years old or older. We assayed total acid phosphatase activities in the presence of a transphosphorylating agent and using alpha-naphthyl phosphate as substrate. The main factors modifying total and tartrate-resistant acid phosphatases activities in serum are similar to those observed for total and bone alkaline phosphatases activities: age, sex, and hormonal state (puberty or menopause). The tartrate-inhibited acid phosphatase activity is, however, independent of biological variations. Finally, we propose reference limits for total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum.

Acid Phosphatase↗

PubMed1992

Conversion of skeletal tartrate-sensitive acid phosphatases into tartrate-resistant isoenzymes in vitro.

1. Chicken skeletal tartrate-sensitive (TsACP) and -resistant (TrACP) acid phosphatase isoenzymes could be separated from each other by carboxylmethyl-sepharose ion exchange chromatography. 2. Chicken skeletal TsACP showed a gradual time-dependent loss of sensitivity to tartrate inhibition when incubated at room temperature, but not at 4 degrees C. 3. The loss of sensitivity to tartrate inhibition was associated with an activation of the enzyme activity. 4. These changes were accompanied with a shift in the electrophoretic mobility of the enzyme activity from a large molecular sized form to a smaller molecular sized form that resembled the freshly prepared TrACP on the native acidic polyacrylamide electrophoresis gels, and on molecular sieve Superose-12 Fast Protein Liquid Chromatography. 5. Kinetic evaluations of the biochemical properties of the "converted" TsACP activity resembled the TrACP. 6. The apparent "conversion" was not unique to chicken TsACP, since similar "conversion" was observed with partially purified preparations of bovine bone matrix TsACP and of human osteoblastic TsACP. 7. Addition of several serine protease inhibitors did not prevent the "conversion". 8. These findings are consistent with the possibility that skeletal TsACPs are precursors of skeletal TrACPs.

Acid Phosphatase↗

PubMed1990

Histochemistry and biochemistry of tartrate-resistant acid phosphatase (TRAP) and tartrate-resistant acid adenosine triphosphatase (TrATPase) in bone, bone marrow and spleen: implications for osteoclast ontogeny.

In order to evaluate the usefulness of a recently described acid ATPase as a marker for osteoclast differentiation, we have performed histochemical and biochemical analyses of the distribution of tartrate-resistant acid phosphatase (TRAP) and tartrate-resistant acid ATPase (TrATPase) in bone, bone marrow and spleen. Histochemical studies of bone demonstrated that multinucleated osteoclasts stained for both TRAP and TrATPase. However, staining for TRAP covered the entire cytoplasm, whereas TrATPase staining was localized primarily to cytoplasmic areas next to bone and on adjacent mineralized surfaces. Occasionally TrATPase-positive mononuclear cells were observed on excavations in the bone surface. In the spleen, mononuclear TRAP-positive cells were located in the marginal zone between the white and red pulp, whereas no staining for TrATPase was observed. Comparison of the biochemically measured TRAP and TrATPase activities showed that bone had the highest specific activity for both enzymes followed by the bone marrow and spleen. However, enzyme activity in the spleen compared to bone was about 4-fold higher for TRAP compared to TrATPase. Additional evidence for a restricted expression of TrATPase to bone relative to spleen was obtained by in vitro translation studies. These data indicate that TrATPase is a more selective marker than TRAP in histochemical and biochemical studies of osteoclast differentiation and furthermore suggest that development of TrATPase is a late acquisition in osteoclast ontogeny.

Acid Phosphatase↗

PubMed2004

Characterization and in vitro degradation of poly(2,3-(1,4-diethyl tartrate)-co-2,3-isopropyliden tartrate).

In the present study, a less known polyester based on tartaric acid was characterized with respect to its degradation mechanism. Poly(2,3-(1,4-diethyl tartrate)-co-2,3-isopropyliden tartrate) (PTA) differs from commonly used biodegradable polyesters, such as poly(lactides-co-glycolides) (PLGA) by the presence of additional cleavable bonds in the polymer side chains. This modification results in different polymer properties and influences polymer degradation. The hydrolytic degradation of PTA was studied in parallel to PLGA using disc-shape matrices, which were obtained by compression-molding. The discs were incubated in pH 7.4 phosphate buffer solution at 37 degrees C. The degraded samples were characterized for percentage mass loss, water absorption, decay of molecular weight and change in glass transition temperature. The results demonstrate that the degradation of PTA proceeds via bulk erosion similar to PLGA. However, the degradation of PTA implants is characterized by a rapid mass loss within a short period of time appearing after a definite lag phase without remarkable mass loss. This makes the polymer promising for pulsatile drug release systems.

Alkenes↗

PubMed1987

Clinical significance of tartrate-sensitive and tartrate-resistant acid phosphatase indicated from the study of their biosynthetic mechanism.

The tartrate-sensitive prostatic acid phosphatase, bands 2 and 4, are found in the soluble cytosol, and absent in the polysome of the prostate, while the tartrate-resistant acid phosphatase band 5 is present in the polysome and the soluble cytosol of hairy cells. The mRNA isolated from the prostate catalyzes the incorporation of 3T leucine into a protein different from that of bands 2 and 4. On the other hand, the mRNA isolated from the hairy cells catalyzes the incorporation of 3T leucine into band 5. The different biosynthetic mechanism of these two types of acid phosphatases are discussed in light of their different clinical significance.

Acid Phosphatase↗

PubMed1957