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PubMed2002

Dosimetric characteristics of Li2B4O7:Cu,Ag,P solid TL detectors.

The main dosimetric characteristics are presented of newly prepared tissue-equivalent, highly sensitive thermoluminescent detector, Li,B4O7:Cu,Ag,P in the form of sintered pellets, developed at the Institute of Nuclear Sciences, Vinca. As a result of an advancement in the preparation procedure by the sensitising of basic copper activated lithium borate TL material, significant improvement in the TL sensitivity of Li2B4O7:Cu,Ag,P was gained. The glow curve of Li,B4O7:Cu,Ag,P consists of well defined main dosimetric peak situated at about 185-190 degrees C with the TL sensitivity which is about four to five times higher than that of LiF:Mg,Ti (TLD-100). From the experimental results a very wide linear dose response range, up to 10(3) Gy is evident. Dosimetric characteristics make sintered solid Li,B4O7:Cu,Ag,P TL detectors very promising for different dosimetry applications particularly in medical dosimetry and also for individual monitoring.

Borates↗
PubMed1985

Regeneration in Alfalfa Tissue Culture: Characterization of Intracellular pH During Somatic Embryo Production by Solid-State P-31 NMR.

The composition of phosphorus-containing compounds of intact lyophilized alfalfa tissue has been determined, in part, by solid-state (31)P nuclear magnetic resonance. The tissue (Medicago sativa L., cv Regen S; and some of its crosses) was grown in culture under both nonregenerating and regenerating conditions, the latter enhanced by the addition of specific amino acids. Analysis of the (31)P nuclear magnetic resonance spectra shows that regeneration is favored when metabolism occurs without the production of a low average intracellular pH.

Journal Article↗
PubMedDate not supplied

pH imaging. A review of pH measurement methods and applications in cancers.

Acid-base balance is altered in a variety of common pathologies, including COPD, ischemia, renal failure, and cancer. Because of robust cellular pH homeostatic mechanisms, most of the pathological alterations in pH are expressed as changes in the extracellular, systemic pH. There are data to indicate that altered pH is not simply an epiphenomenon of metabolic or physiologic imbalance but that chronic pH alterations can have important sequelae. MRSI and MRI measurements indicate that pH gradients of up to 1.0 pH unit can exit within 1-cm distance. Although measurement of blood pH can indicate systemic problems, it cannot pinpoint the lesion or quantitatively assess the magnitude of excursion from normal pHe. Hence, there is a need to develop pHe measurement methods with high spatiotemporal resolution. The two major approaches being investigated include magnetization transfer methods and relaxation methods. pH-dependent MT effects can observed with endogenous signals or exogenously applied CEST agents. While endogenous signals have the advantage of being fully noninvasive and relatively straightforward to apply, they lack a full biophysical characterization and dynamic range that might be afforded by future CEST agents. pH-dependent relaxivity also requires the injection or infusion of exogenous contrast reagents. In both MT and relaxographic approaches, the magnitude of the effect, and, thus, the ability to quantify pHe, depends on a spatially and temporally varying concentration of the CR. A number of approaches have been proposed to solve this problem and, once it is solved, pH imaging methods will be applicable to human clinical pathologies.

Acid-Base Equilibrium↗
PubMed1988

Synthesis of a tripeptide with a C-terminal nitrile moiety and the inhibition of proteinases.

The synthesis of the tripeptide D-Phe-Pro-Arg with the nitrile group instead of the carboxylgroup is described. Initially, the corresponding peptide amide was synthesized by conventional methods in solution using Boc and Fmoc as the protecting group for D-Phe. The dehydration in order to create the nitrile moiety was achieved by treating the peptide amide with phosphorus oxichloride or trifluoroacetic anhydride. Best results were obtained by the use of phosphorus oxichloride in pyridine as the solvent in the presence of imidazole. After deprotection of the N-terminal amino acid the crude product was purified by chromatography on Butyl-Fractogel HW-40 (S). The purity of the final product was checked on a RP18 phase by hplc. The existence of the nitrile group was demonstrated by i.r. and 13C-n.m.r. spectra. The peptide nitrile exhibited a strong inhibition of thrombin compared to the tripeptide amide.

Acetic Anhydrides↗
PubMed1996

Side reactions in the pyroglutamic acid-7-amino-4-methylcoumarin synthesis.

N-Formylpyroglutamic acid-7-amido-4-methylcoumarine and pyroglutamyl-pyroglutamic acid-7-amido-4-methylcoumarin are the major products in the synthesis of pyroglutamic acid-7-amido-4-methylcoumarin by phosphorus pentachloride in dimethylformamide and dicyclohexylcarbodiimide under pyridine activation.

Chlorides↗
PubMed2005

One pot conjugation of the polypeptides directed by phosphorus oxychloride.

A series of homopeptides and their conjugates were synthesized in one pot reaction in the presence of phosphorus oxychloride and the conjugate yield was structurally dependent. Menthol and benzylamine conjugated to the homopeptides quantitatively. Homopeptides when treated with diisopropyloxyphosphite (DIPPH) and NaClO yield the corresponding N-phosphoryl peptides. Electrospray ionization-mass spectrometry (ESI-MS)/MS was used to study the structure of peptide conjugates. This paper reports a simple method to synthesize the homopeptides and their conjugate derivatives and the fact that phosphoryl peptides could also be obtained by one pot reaction.

Benzylamines↗
PubMed1975

31P nuclear-magnetic-resonance studies of pyridoxal and pyridoxamine phosphates. Interaction with cytoplasmic aspartate transaminase.

The 31P nuclear magnetic resonance (NMR) spectrum of the phosphate in free pyridoxal or pyridoxamine phosphate reveals a resonance signal that is coupled to the methylene protons of the 5-CH2 with JHP of 6.0 +/- 0.3 Hz. Proton noise decoupling results in a single signal with a pH-dependent chemical shift with deprotonation of the phosphate resulting in a shift of the 31P resonance to lower fields. A single 31P NMR signal at a frequency corresponding to fully ionized phosphate monoesters is observed in aspartate-transaminase-bound pyridoxal or pyridoxamine phosphate. The 31P resonance in the holotransaminase is pH-independent and is unaffected by saturating concentrations of substrates or inhibitors. Only denaturation with 6 M guanidine with HCl results in changes in the 31P of the holoenzyme. It appears that the phosphate group of pyridoxal phosphate is bound to a positive pocket in the holoenzyme and remains fully ionized in the pH range of 5.6 to 9.2. The phosphate-binding properties are present even in the apoenzyme which is able to bind inorganic phosphate which then can be displaced by pyridoxal or pyridoxamine phosphate in the process of holoenzyme formation.

Animals↗
PubMed1984

31P-NMR studies of the freeze-tolerant larvae of the gall fly, Eurosta solidaginis.

31P NMR was applied to an examination of the freeze-tolerant larvae of the gall fly, Eurosta solidaginis. Resonances from sugar phosphates, inorganic phosphate, adenylates and arginine phosphate were identified. Two peaks of Pi were identified corresponding to intracellular and extracellular Pi. Anoxia produced an expected decrease in peak intensities of ATP and arginine phosphate while the peak of intracellular Pi was enhanced and shifted to indicate intracellular acidification during anoxia. Spectra of whole larvae were monitored over a temperature range from -30 degrees to +25 degrees C. No abrupt alterations in the spectra were seen at the point of extracellular freezing which occurs at about -8 degrees C but temperature had dramatic effects upon the peak intensities of ATP and arginine phosphate. A reversible increase/decrease in peak intensities, relative to Pi, was observed as temperature was raised/lowered. At 15 degrees and -20 degrees C, the beta peak of ATP was 64% and 2% of the peak intensity of Pi while that of arginine phosphate was 78% and 11%, respectively. This temperature effect was not an artifact of instrumentation (as model solutions containing Pi, ATP and arginine phosphate did not show this effect) or a result of changes in the total amounts of these compounds in the cell with temperature. Rather it is apparent that these molecules become restricted in their rotational movement as temperature is lowered perhaps via binding to subcellular components. Changes in the amounts of freely soluble ATP and arginine phosphate with temperature could have important implications for metabolism and its control. Analysis of the effect of temperature on the chemical shift of Pi was also used to determine pH in the intracellular and extracellular compartments. Temperature change had no effect on extracellular (hemolymph) pH which remained constant at 6.1-6.3. Intracellular pH varied with temperature, however, from pH 6.8 at 15 degrees C to pH 7.3 at -12 degrees C with a change, delta pH/delta 0, of -0.0185 degrees C consistent with alphastat regulation.

Adenosine Triphosphate↗
PubMed1989

Effect of ADP on the rate of acetyl phosphate hydrolysis by the Ca2+-ATPase of sarcoplasmic reticulum.

Hydrolysis of acetyl phosphate is inhibited by high concentrations of Pi and MgCl2, probably due to an increase in the steady-state level of phosphoenzyme formed from Pi in the medium. A dual effect of ADP during steady-state hydrolysis of acetyl phosphate was observed. ADP inhibited hydrolysis in the presence of 5 mM MgCl2 and no added Pi, whereas it stimulated hydrolysis when phosphoenzyme formation by Pi was favored by including 6 mM Pi and 20 mM MgCl2 in the assay medium. ATP inhibited acetyl phosphate hydrolysis in both of these assay media. When phosphoenzyme formation by Pi in the presence of acetyl phosphate was stimulated at Ca2+ concentrations sufficient to saturate the low-affinity Ca2+-binding sites, ADP stimulated acetyl phosphate hydrolysis and also promoted ATP synthesis by reversal of the catalytic cycle. The rate of ATP synthesis was dependent on ADP, Pi and Ca2+. Phosphoenzyme formation by Pi and MgCl2, whether in the absence of Ca2+ and acetyl phosphate, or during acetyl phosphate hydrolysis, was inhibited by ADP and ATP. These results suggest that ADP interacts with different intermediates of the catalytic cycle and that expression of inhibition or activation of acetyl phosphate hydrolysis depends on the steady-state level of phosphoenzyme formed by Pi.

Adenosine Diphosphate↗
PubMed1991

Kinetic studies of the variations of cytoplasmic pH, nucleotide triphosphates (31P-NMR) and lactate during normoxic and anoxic transitions in maize root tips.

We have followed the dynamic evolution of intracellular pH and of the intracellular concentration of nucleotides (NDP, NTP), Pi and lactate in maize root tips during the course of normoxia and anoxia transition. The intracellular pH, determined from the 31P-NMR chemical shift of the cytoplasmic P1 peak, dropped from 7.5 to 6.9 during the first few minutes after anaerobiosis. It increased again, then settled to a steady-state value of 7.1-7.2, 25 min after the beginning of the anoxic treatment. Following oxygenation, the chemical shift of the cytoplasmic Pi peak drifted gradually to its initial value. The cytoplasmic pH followed an oscillatory time course which was almost identical to the time course of NTP. Intracellular lactate accumulated steadily during the first 30 min after anaerobiosis, then its intracellular concentration remained almost constant. Following oxygenation, the intracellular concentration of lactate decreased slowly. The cytoplasmic pH followed a time course which was not identical to the time course of lactate. Following hypoxia, the pH dropped to low values long before the intracellular lactate concentration reached a steady-state equilibrium. Conversely, subsequent to oxygenation, the pH returned to normal values long before lactate. These results do not agree with the statement that cytoplasmic acidification in hypoxic maize root tips is necessarily associated with lactic acid synthesis.

Cytoplasm↗
PubMed1981

Match dermatitis.

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Dermatitis, Contact↗