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PubMed2002

Thermoluminescence properties of LiF:Mg,Cu,Na,Si pellets in radiation dosimetry.

Sintered LiF:Mg,Cu,Na,Si thermoluminescence (TL) pellets have been developed for application in radiation dosimetry. LiF:M,Cu,Na,Si TL pellets were made from TL powders using a sintering process, that is, pressing and heat treatment. These pellets have a diameter of 4.5 mm, and a thickness of 0.8 mm are blue in colour and have a mass of 28 mg each. After 400 pellets had been produced they were irradiated with 137Cs gamma radiation and samples having a sensitivity within a +/-5% standard deviation were selected for experimental use. In the present study, the physical and dosimetric properties of LiF:Mg,Cu,Na,Si TL pellets were investigated for their emission spectrum, dose response, energy response and fading characteristics. Photon irradiation for the experiments was carried out using X ray beams and a 137Cs gamma source at the Korea Atomic Energy Research Institute (KAERI). The average energies and the dose were in the range of 20-662 keV and 10(-6) - 10(2) Gy respectively. The glow curves were measured with a manual type thermoluminescence dosimetry reader (system 310, Teledyne) at a constant nitrogen flux and a linear heating rate. For a constant heating rate of 5 degrees C.s(-1). the main dosimetric peak of the glow curve appeared at 234 degrees C, its activation energy was 2.34 eV and the frequency factor was 1.00 x 10(23). The TL emission spectrum appeared at the blue region centred at 410 nm. A linearity of photon dose response was maintained up to 100 Gy. The photon energy responses relative to the 137Cs response were within +/-20% in the overall photon energy region. No fading of the TL sensitivity of the pellets stored at room temperature was found over the course of a year. Therefore LiF:Mg,Cu,Na,Si TL pellets can be used for personal dosimetry, but more research is needed to improve the characteristics for repeated use.

Copper↗
PubMed2002

A new paradigm in personal dosimetry using LiF:Mg,Cu,P.

The United States Navy has been monitoring personnel for occupational exposure to ionising radiation since 1947. Film was exclusively used until 1973 when thermoluminescence dosemeters were introduced and used to the present time. In 1994, a joint research project between the Naval Dosimetry Center, Georgetown University, and Saint Gobain Crystals and Detectors (formerly Bicron RMP formerly Harshaw TLD) began to develop a state of the art thermoluminescent dosimetry system. The study was conducted from a large-scale dosimetry processor point of view with emphasis on a systems approach. Significant improvements were achieved by replacing the LiF:Mg,Ti with LiF:Mg,Cu,P TL elements due to the significant sensitivity increase, linearity, and negligible hiding. Dosemeter filters were optimised for gamma and X ray energy discrimination using Monte Carlo modelling (MCNP) resulting in significant improvement in accuracy and precision. Further improvements were achieved through the use of neural-network based dose calculation algorithms. Both back propagation and functional link methods were implemented and the data compared with essentially the same results. Several operational aspects of the system are discussed, including (1) background subtraction using control dosemeters, (2) selection criteria for control dosemeters, (3) optimisation of the TLD readers, (4) calibration methodology, and (5) the optimisation of the heating profile.

Algorithms↗
PubMed2003

Effect of minerals on activity of microbial uricase to reduce ammonia volatilization in poultry manure.

Inhibition of microbial uricase in poultry manure is critical to reduce NH3 volatilization, because hydrolysis of uric acid by microbial uricase is the first step in the production of NH3 gas in poultry manure. Three experiments were conducted to evaluate the effects of minerals on uricase activity and NH3 volatilization from poultry manure. In Experiment 1, an in vitro enzyme assay was used to evaluate the effects of Zn, Cu, Mg, and Mn on the activity of microbial uricase. There were three treatments: uricase, uricase + minerals, and uricase preincubated with minerals. Uric acid concentration was measured at 293 nm with a spectrophotometer. The results indicated that Zn and Cu greatly blocked the activity of microbial uricase (>90% inhibition), whereas Mg and Mn were less inhibitory. Experiment 2 was designed to evaluate the effect of ZnSO4 on the growth of uric acid-utilizing microorganisms by an in vitro assay. There were three treatments: control, ZnSO4 (10 mM), and ZnSO4 (50 mM). The results indicated that ZnSO4 significantly reduced the number of uric acid-utilizing microorganisms compared to the control. In Experiment 3, an NH3-trapping system was used to evaluate the effect of different levels of ZnSO4 on NH3 volatilization and nitrogen retention in poultry manure. Poultry manure (300 g) was mixed with 0, 0.15, 0.3, 1.5, 3, or 6 g ZnSO4 to create manure concentrations of Zn at 0, 0.05, 0.1, 0.5, 1, or 2% (wt/wt), respectively. The 1 and 2% ZnSO4 treatments significantly increased manure uric acid and total nitrogen retention by reducing NH3 volatilization compared to the control during the 3-wk incubation.

Ammonia↗
PubMed2004

Developments in the synthesis of LiF:Mg,Cu,Na,Si TL material.

A procedure for synthesis of the highly sensitive pellet-type LiF:Mg,Cu,Na,Si thermoluminescent (TL) detector has been newly developed. It was found that the optimum concentrations of dopants for a pellet-type LiF:Mg,Cu,Na,Si TL detector were found to be Mg: 0.2 mol %, Cu: 0.05 mol %, Na: 0.9 mol%, and Si: 0.9 mol%. The TL sensitivity of this new detector was about 30 times higher than that of the TLD-100 by light integration measurements. Reusability study of the detector was carried out for 10 cycles. The results show that the coefficients of variation for each detector separately did not exceed 0.016, and that for all 10 detectors collectively was 0.0054.

Copper↗
PubMed1979

Phosphonoformate inhibits reverse transcriptase.

The new antiviral substance phosphonoformate (PFA) has been tested in a cell-free system for its effect on reverse transcriptases from an avian retrovirus (avian myeloblastosis virus, AMV) and from mammalian retroviruses (Rauscher leukaemia virus, RMuLV; bovine leukaemia virus; baboon endogenous virus; simian sarcoma virus; visna virus). The observed inhibitory effect of PFA has been compared with that of a structurally related substance, phosphonoacetate (PAA). Phosphonoformate, at a concentration of 100 microM, reduced the activities of all the above mentioned polymerases by 90% when (rA)n.(dT)10 was used as a template/primer. The dose-response curves for AMV and RMuLV polymerases primed with (rA)n.(dT)10 showed PFA to be a 1000-fold more active than PAA; the RMuLV polymerase activity was reduced to 50% after incubation with 0.7 microM-PFA and 0.7 mM-PAA, respectively. There was no difference in PFA inhibition of virus-associated and purified reverse transcriptase activity. Results with various synthetic templates showed that both the RNA- and the DNA-dependent polymerase activities of reverse transcriptase were inhibited by PFA. The endogenous polymerase activity of AMV was inhibited to 50% at 100 microM-PFA, while PAA had no effect. The PFA inhibition was dependent on whether Mg2+ or Mn2+ was used as divalent cation in the assay. Phosphonoformate arrested DNA synthesis immediately after being added to the assay system. The mechanism of inhibition of the AMV polymerase was non-competitive with respect to substrate and template and the apparent inhibition constants were 16 microM and 9 microM, respectively.

Animals↗
PubMed1975

Purification and characterization of a polyphosphate kinase from Arthrobacter atrocyaneus.

Polyphosphate kinase, an enzyme which incorporated the gamma-phosphate of ATP into long-chain polyphosphate molecules, was purified more than 700-fold from Arthrobacter atrocyaneus by ammonium sulphate fractionation, DEAE-cellulose column chromatography and Ssphadex G-200 gel filtration. The enzyme had a broad pH optimum at 6-0 to 7-0 and required Mn2+ or Mg2+, histone, and inorganic phosphate for activity. The Km for Mn-ATP was 0-53 mM, and for inorganic phosphate was 1-67 mM. Free ATP concentrations greater than 8 muM inhibited the enzyme. Free Mn2+ or Mg2+ concentrations greater than 2 mM or 6 mM, respectively, were also inhibitory. Activity was strongly inhibited by 4 mM-ADP, 1 mM-PP1 or 20 mM-NaF. The effect of ADP might have resulted from reversing the equilibrium of the kinase reaction. The activation by phosphate ions might indicate a role for the enzyme in regulating intracellular phosphate levels or maintaining a phosphorus reserve. The level of enzymic activity in the bacteria responded to changes in inorganic phosphate concentration in the medium. Basic proteins, such as protamine, could substitute for histone as activator. Proteins such as casein or bovine serum albunim would also substitute for histone but only in the absence of inorganic phosphate. The presence of a protein might be necessary to form a complex with the product, thus preventing reversal of the reaction in vitro. The reaction product was characterized, and found to be labile in hydroxylamine, base, and acid at 100 degrees C. It behaved as a long-chain-polyphosphate molecule on chromatography in an Ebel's solvent. The enzymic activity was therefore not that of a protein kinase.

Adenosine Triphosphate↗
PubMed2005

NH4+ currents across the peribacteroid membrane of soybean. Macroscopic and microscopic properties, inhibition by Mg2+, and temperature dependence indicate a SubpicoSiemens channel finely regulated by divalent cations.

The control of ammonium (NH(4)(+)) transport is critical in preventing futile cycles of NH(4)(+)/ammonia transport. An unusual nonselective cation channel with subpicoSiemens single-channel conductance permeable to NH(4)(+) had previously been identified in the peribacteroid membrane (PBM) of symbiosomes from soybean (Glycine max) nodules. Here, we investigate the proposed channel mechanism and its control by luminal magnesium. Currents carried by NH(4)(+) were measured in inside-out PBM patches by patch clamp. NH(4)(+) transport corresponding to the physiological direction of net transfer showed time-dependent activation and associated single-channel-like events. These could not be resolved to discrete conductances but had the same selectivity as the total current. The voltage dependence of the steady-state current was affected by temperature consistent with the rate constant of channel opening being reduced with decreased temperature. This resulted in steady-state currents that were more temperature sensitive at voltages where the current was only partially activated. When fully activated, the current reflected more the ion conduction through open channels and had an activation energy of 28.2 kJ mol(-1) (Q10 = 1.51, 8 degrees C-24 degrees C). Increased Mg(2+) on the symbiosome lumen side blocked the current (ID(50) = 351 microm, with 60 mm NH(4)(+)). Complete inhibition with 2 mm Mg(2+) was relieved with a small increase in NH(4)(+) on the lumen side of the membrane (shift of 60-70 mm). With Mg(2+) the selectivity of the transport for divalent cations increased. From these features, we propose a divalent-dependent feedback regulation of the PBM-nonselective cation channel that could maintain a constant NH(4)(+) gradient across the membrane.

Biological Transport, Active↗
PubMed1995

Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphatase activity.

A pea (Pisum sativum L.) nuclear enzyme with protein tyrosine phosphatase activity has been partially purified and characterized. The enzyme has a molecular mass of 90 kD as judged by molecular sieve column chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Like animal protein tyrosine phosphatases it can be inhibited by low concentrations of molybdate and vanadate. It is also inhibited by heparin and spermine but not by either the acid phosphatase inhibitors citrate and tartrate or the protein serine/threonine phosphatase inhibitor okadaic acid. The enzyme does not require Ca2+, Mg2+, or Mn2+ for its activity but is stimulated by ethylenediaminetetraacetate and by ethyleneglycolbis(beta-aminoethyl ether)-N,N'-tetraacetic acid. It dephosphorylates phosphotyrosine residues on the four different 32P-tyrosine-labeled peptides tested but not the phosphoserine/threonine residues on casein and histone. Like some animal protein tyrosine phosphatases, it has a variable pH optimum depending on the substrate used: the optimum is 5.5 when the substrate is [32P]tyrosine-labeled lysozyme, but it is 7.0 when the substrate is [32P]tyrosine-labeled poly(glutamic acid, tyrosine). It has a Km of 4 microM when the lysozyme protein is used as a substrate.

Calcium Chloride↗
PubMed1990

The ATPase of Bacillus alcalophilus. Purification and properties of the enzyme.

The ATPase of Bacillus alcalophilus was extracted from the bacterial membranes with Triton X-100 and purified by hydroxyapatite column chromatography. SDS gel-electrophoresis of the purified protein indicated the typical subunit pattern of an F1F0 structure with five F1 subunits (alpha, beta, gamma, delta, epsilon) and three F0 subunits (a,b,c). The alpha and beta subunits were antigens for an antiserum against the corresponding subunits of the ATPase of Escherichia coli. Subunit c was extracted from the bacterial membranes with chloroform/methanol. Its amino acid composition was in the range of subunits c from other ATPases. Maximal ATPase activity was observed in the presence of 2-5 mM MgCl2, an ATP/Mg2+ ratio of 2:1 and 25% methanol. In the absence of methanol, only about 1% of the maximal activity was observed. The enzyme was also activated by Ca2+ (in the absence of methanol), reaching about 30% of the maximal activity. The dependence of initial velocity versus ATP of the Ca2(+)-activated but not of the Mg2+/methanol-activated enzyme indicted cooperativity with three strongly cooperative binding sites.

Adenosine Triphosphatases↗
PubMed1992

Human placental alkaline phosphatase. An improved purification procedure and kinetic studies.

An improved method for the purification of human placental alkaline phosphatase is described. The partially purified enzyme from Sigma was further purified by successive Concanavalin A-Sepharose and Q-Sepharose chromatography. The whole procedure may be completed in one working day. Highly purified enzyme was obtained with a 39% yield. The intrinsic fluorescence of the enzyme decreased at elevated temperature. The conformation of the enzyme molecule was studied by the fluorescence quenching technique. Upward Stern-Volmer plots were obtained for the quenching data which suggested that, in addition to collisional quenching, static quenching was involved in the quenching mechanism. The dynamic and static quenching constants were found to be 0.7 +/- 0.16 M-1 and 0.44 +/- 0.1 M-1, respectively, using acrylamide as the quenching agent. The corresponding values were 0.43 +/- 0.23 M-1 and 0.84 +/- 0.18 M-1, respectively, with KI as the quenching agent. Mg2+ and PO4(3-) induced protein conformational changes which altered both the dynamic and static quenching constants. Mg2+ was found to be a non-essential activator for the placental alkaline-phosphatase-catalyzed hydrolysis of 4-nitrophenyl phosphate. At pH 9.8, Mg2+ increased Vmax by 1.2-fold without affecting the Kd of the substrate. The tetranitromethane-modified enzyme showed slower migration toward the anode on electrophoresis and increased Kd for Mg2+.

Alkaline Phosphatase↗
PubMed1994

Effects of divalent cations on adenosine agonist binding to A1 receptors and non-A1/non-A2 sites in rat cerebral cortex.

In the present study results are reported concerning the effects of several divalent cations on the binding characteristics of [3H]-cyclohexyladenosine on A1 adenosine receptors and of [3H]-N-ethylcarboxamidoadenosine on non-A1/non-A2 sites in membranes from cerebral cortex of the rat. The [3H]-cyclohexyladenosine binding to A1 receptors was dose-dependently increased by Mn2+, Co2+, Ca2+. The binding characteristics of the agonist were differently affected by Ca2+/Mn2+ and Mg2+. Ca2+ and Mn2+ increased the Bmax value without any change in Kd, whereas Mg2+ decreased the Kd value without changing the Bmax. In the presence of Ca2+ and Mg2+ the Kd value was similar to that obtained in the presence of Mg2+, whereas the Bmax value was similar to the apparent number of binding sites calculated in the presence of Ca2+. The cations, Cu2+, Cd2+, Zn2+, decreased the A1 binding with IC50 values of 19.6 microM, 39.2 microM and 103.9 microM, respectively. The binding characteristics of [3H]-N-ethylcarboxamidoadenosine to non-A1/non-A2 sites were affected by Ca2+, Mn2+, Co2+ and Mg2+ in the opposite manner to A1 receptors. They decreased the binding with IC50 values of 20.1 mM, 22.8 mM, 93.0 mM and 18.1 mM, respectively. This occurs through an enhancement in Kd values without changes in the number of binding sites. The findings on A1 receptor and non-A1/non-A2 binding site, taken together, suggest that cations could also exert a modulatory action via specific interactions with divalent cation binding sites on the receptor molecule.

Adenosine↗
PubMed1968

Flagellar adenosine triphosphatase from sea urchin sperm: properties and relation to motility.

Adenosine triphosphatase activated by divalent cations is apparently a component of the motile apparatus in flagella of Arbacia sperm, as judged by the activity of this enzyme in intact flagella, glycerol-extracted flagella, and soluble extracts prepared from flagella. However, the variation in the physical properties and in the amount of enzyme obtained after a variety of treatments suggests that additional components are involved in the motile mechanism. These features distinguish the soluble flagellar enzyme from adenosine triphosphatases of other motile cells.

Adenosine Triphosphatases↗
PubMed1996

Mapping of catalytic residues in the RNA polymerase active center.

When the Mg2+ ion in the catalytic center of Escherichia coli RNA polymerase (RNAP) is replaced with Fe2+, hydroxyl radicals are generated. In the promoter complex, such radicals cleave template DNA near the transcription start site, whereas the beta' subunit is cleaved at a conserved motif NADFDGD (Asn-Ala-Asp-Phe-Asp-Gly-Asp). Substitution of the three aspartate residues with alanine creates a dominant lethal mutation. The mutant RNAP is catalytically inactive but can bind promoters and form an open complex. The mutant fails to support Fe2+-induced cleavage of DNA or protein. Thus, the NAD-FDGD motif is involved in chelation of the active center Mg2+.

Amino Acid Sequence↗