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A Lanir

Publications and source records attributed to A Lanir.

At least 19 recordsLinked to original sources
PubMed1992

23Na- and 31P-NMR studies of perfused mouse liver during nitrogen hypoxia.

The effects of nitrogen hypoxia on isolated perfused mouse livers from fed mice were studied at 37 degrees C using 23Na and 31P nuclear magnetic resonance (NMR) spectroscopy. The paramagnetic shift reagent, dysprosium-triethylenetetraminehexaacetic acid, was used to distinguish intracellular from extracellular sodium. The area of the intracellular sodium resonance remained relatively constant over the first 30 min of hypoxia and then increased by a factor of approximately 2 relative to controls over the next 30 min. High-energy phosphate metabolites were measured using 31P-NMR. The beta-ATP resonance decreased to zero, and the intracellular pH decreased from 7.3 to 6.9 during 60 min of hypoxia. Liver enzyme activity in the effluent exiting the liver increased in direct proportion to the length of hypoxia up to 56 min. The sodium, ATP, and enzyme changes during hypoxia were correlated with histological and electron-microscopic findings. The morphology of liver specimens exposed to 30 min of hypoxia was close to normal, whereas extensive centrilobular and midlobular necrosis was seen in specimens subjected to 60 and 90 min of hypoxia. The effect of 30 min of reoxygenation after 15, 30, 45, 60, and 90 min of hypoxia was also studied. The level of beta-ATP recovery depended on the duration of hypoxia. For 60 min of hypoxia followed by reoxygenation, beta-ATP recovered to only 20% of control values. The morphology of hypoxic livers after 30 min of reoxygenation was similar to livers subjected to hypoxia alone.

Animals↗
PubMed1988

Liver adenosine triphosphate and pH in fasted and well-fed mice after infusion of adenine nucleotide precursors.

Nutrition is a factor which may affect the liver energy charge. Experiments were performed to determine the effect of starvation and of ATP precursors, adenine and ribose on liver energy stores. The 31P NMR spectra of well-fed and starved mice livers were studied in a perfusion system using Krebs-Henseleit buffer (KHB). The ATP precursors, adenine (20 mmol/l) and ribose (80 mmol/l), were then added to determine their effect. Their effect on the ATP dynamics during ischemia and reperfusion were then evaluated. The effects of adenine alone and ribose alone were then determined. The 31P spectra of well-fed mice demonstrated high ATP content relative to Pi, phosphoesters and phospholipids. Animals starved for 24 h showed very low ATP, high Pi and little or no detectable phospholipids. In starved animals, ATP rose steadily to approximately 50% above the baseline level when precursors were added. Pi decreased to 30% of the baseline after 40 min. Little change was noted in well-fed animals. The rate of ATP decay did not change with the onset of ischemia, whether the livers were perfused with KHB alone or KHB with precursors. Upon reperfusion, precursors improved the recovery of ATP (81% vs 49% after 20 min ischemia, 44% vs 34% after 30 min ischemia). Addition of adenine alone produced similar results, but addition of ribose alone did not significantly alter ATP recovery. In conclusion, supplying starved or post-ischemic livers with adenine or ribose and adenine does improve ATP levels.

Adenine↗
PubMed1987

Nuclear magnetic resonance assessment of adenosine triphosphate (ATP) dynamics in ischemic mouse livers perfused with adenine and ribose.

Hepatic energy stores are essential to liver viability. We used a mouse liver perfusion model and MR spectroscopy to study the effect of adding two precursors of ATP (adenine and ribose) on ATP dynamics during ischemia and reperfusion. Using Krebs-Henseleit buffer with or without added adenine and ribose made little difference in the ATP decay rate during ischemia, but the recovery of ATP during reperfusion was more complete when adenine and ribose were added to the buffer. These findings suggest that the addition of the precursors of ATP, adenine and ribose, to perfusate after ischemia can accelerate and enhance ATP recovery.

Adenine↗
PubMed1987

Liver preservation for transplant. Evaluation of hepatic energy metabolism by 31P NMR.

31P NMR spectroscopy proved to be an excellent, dynamic, nondestructive method for assessing the liver during cold flush and pulsatile perfusion experiments. 31P NMR spectroscopy was used to measure ATP decay, inorganic phosphate appearance, and phosphate chemical shift in the excised mouse livers subjected to cold and warm ischemia. Cold flush followed by cold preservation in saline, Krebs-Henseleit buffer, or Collins' solution showed that Collins' solution resulted in the slowest ATP decay. In temperature-controlled experiments (5 degrees -37 degrees C), ATP decay was much slower with lower temperature. In separate pulsatile perfusion experiments with oxygenated Krebs-Henseleit buffer, hepatic ATP was unchanged for at least 6 hr at 20 degrees C. At 37 degrees C, the NMR spectrum showed changes in the diphosphoesters region, but the ATP remained stable during the 6-hr perfusion. These studies suggest that for long periods of liver preservation, an adequate perfusion method should be developed.

Adenine↗
PubMed1986

Nuclear magnetic resonance proton imaging of bone pathology.

Thirty-two patients with diversified pathology were examined with a supraconductive NMR imager using spin echo with different TR and TE to obtain T1 and T2 weighted images. They included 20 tumors (12 primary, eight metastasis), six osteomyelitis, three fractures, two osteonecrosis, and one diffuse metabolic (Gaucher) disease. In all cases except for the stress fractures, the bone pathology was clearly visualized in spite of the normal lack of signal from the compact cortical bone. Nuclear magnetic resonance (NMR) imaging proved to be at least as sensitive as radionuclide scintigraphy but much more accurate than all other imaging procedures including computed tomography (CT) and angiography to assess the extension of the lesions, especially in tumors extended to soft tissue. This is due both to easy acquisition of sagittal and coronal sections and to different patterns of pathologic modifications of T1 and T2 which are beginning to be defined. It is hoped that more experience in clinical use of these patterns will help to discriminate between tumor extension and soft-tissue edema. We conclude that while radionuclide scintigraphy will probably remain the most sensitive and easy to perform screening test for bone pathology, NMR imaging, among noninvasive diagnostic procedures, appears to be at least as specific as CT. In addition, where the extension of the lesions is concerned, NMR imaging is much more informative than CT. In pathology of the spine, the easy visualization of the spinal cord should decrease the need for myelography.

Adolescent↗
PubMed1979

A Raman spectroscopic study of the interaction of divalent metal ions with adenine moiety of adenosine 5'-triphosphate.

Raman spectra of ATP at various pH values are affected by addition of equimolar solution of divalent metal ions such as Ca2+, Mg2+, Co2+, Cu2+, and Hg2+. The changes in frequency and intensity have been used to construct models describing the nature of metal-adenine and metal-triphosphate interactions under different conditions. The metal ions are found to co-ordinate the triphosphate group in the entire pH range studies (pH to 12). Calcium (II) and magnesium (II) interact strongly with the phosphate moiety at neutral pH, although a weak interaction with the ring occur at low pH values. Around neutrality, several Raman spectral changes are observed to implicate the interaction of cobalt (II) ion with the five-membered ring of the adenine. The changes in Raman frequency are too small to suggest a direct Co(II)-N7 binding. At least six different Cu(II)-ATP species are identified between pH 3 and 12. At pH approximately 7.0 Raman data are explained better by Cu(II) interacting with N7 simultaneously with the amino group of the adenine ring. However, a Cu(II) binding to N3 at pH 10 to 11 is indicated by the enhancement of the 760 and 1360 cm-1 vibrations. At neutral pH, mercury (II) ion shows a direct coordination at N1 while at low pH with N1 blocked by protonation, mercury (II) does not interact with the adenine moiety.

Adenine↗
PubMed1979

Conformational transitions and vibronic couplings in acid ferricytochrome c: a resonance Raman study.

Resonance Raman spectral changes in ferricytochrome c as a function of pH between 6.7 and 1.0 are reported and the structural implication is discussed in terms of the "core-expansion" model advanced by L. D. Spaulding et al. [(1975) J. Am. Chem. Soc. 97, 2517]. The data are interpreted as indicating the iron in high-spin ferricytochrome c (at pH 2.0) with two water molecules as axial ligands lies in the plane of the porphyrin ring. At pH 1.0 there is a different high-spin form of cytochrome c which has an estimated iron out-of-plane distance of approximately 0.46 A. The effect of a monovalent anion at pH 2.0 is to produce a thermal spin mixture with predominant low-spin species. Excitation at approximately 620 nm in acid cytochrome c (pH 2.0) enhances only three depolarized ring vibrations at 1623, 1555, and 764 cm-1. Marked enhancement of depolarized modes relative to polarized and anomalously polarized modes is attributed to the vibronic coupling between porphyrin pi leads to pi and porphyrin pi leads to iron (dpi) charge-transfer states.

Animals↗
PubMed1978

Direct observation of the methionine residues of cytochrome c by 13C nuclear magnetic resonance spectroscopy.

The two Cepsilon-methyl methionine groups in cytochrome c have been chemically enriched (45%) with 13C. Their 13C NMR signals have been monitored in both the oxidized and reduced states and under various solution conditions. Methionine residue 80 showed characteristic chemical shift positions for the reduced Fe(II) and cyano-Fe(III) forms. No signal for methionine 80 was observed in the oxidized Fe(III) form due to the paramagnetic effect of the iron atom to which it is bonded, but the position of the methionine 65 signal was shifted, indicating that it is sensitive to the change of oxidation state. Two well resolved signals were observed at pH 11 for the Fe(III) form but only one was resolved at pH 2, indicating that while methionine 80 is definitely displaced from the iron atom at alkaline pH, it may not be in acid conditions.

Cytochrome c Group↗
PubMed1977

Electron spin relaxation time of Fe(III) in high spin heme proteins.

The electron spin relaxation time of high spin Fe(III), taus, was determined from the frequency dependence (5-100 MHz) of the longitudinal proton relaxation rates of water in solutions of catalase, metmyoglobin and acid ferricytochrome c. In all three high-spin heme proteins the relaxation rates incrased below 25 MHz, while no frequency dependence was observed above that frequency. The results are interpreted by assuming that taus, which modulates the dipolar interaction between the unpaired electrons of the iron and the water protons, is frequently independent. Its value was determined to be (6 +/- 1) - 10(-11) s.

Animals↗
PubMed1976

A nuclear magnetic resonance study of the heme environment in beef liver catalase.

The effect of high-spin heme iron in beef liver catalase on the longitudinal and transverse proton relaxation rates of the solvent has been used to probe the environment of the paramagnetic center. The longitudinal proton relaxation rates were measured as a function of temperature (5-31 degrees C), frequency (5-100 MHz), and pH. T1p was found to be pH independent in the range 6-11, indicating that no significant difference occurs in the heme surrounding within this pH range. The ligands formate and acetate, which preserve the spin state of the heme iron upon ligation, displace a water molecule from the sixth coordination position. This reaction is pH independent, while the binding measured by optical spectroscopy is pH dependent. The electron methanol and ethanol essentially do not change the proton relaxation rates. The temperature and frequency dependencies indicate that the relaxation times are governed by the electronic relaxation time of the high-spin ferric iron tau s. Tau s, which was found to be frequency independent, could not be determined from the T1p/T2p ratio, but only from the frequency dependence of the longitudinal relaxation rate at low frequencies. The results of the least-squares fit of the data to the theory indicate that there is one iron-bound rapidly exchanging water molecule. For the Fe3+ ion it was determined that tau s = 7 x 10(-11) s.

Animals↗
PubMed1975

Temperature and requency dependence of solvent proton relaxation rates in solutions of manganese(II) carbonic anhydrase.

Longitudinal and transverse proton relaxation rates of water in solutions of manganese(II) bovine carbonic anhydrase have been measured by pulsed nuclear magnetic resonance spectrometry as a function of temperature (2-35 degrees), frequently (5-100 MHz) and pH. The pH dependence of the longitudinal relaxation rate was fitted to a sigmoidal curve with a pK value at 7.8, while the esterase activity of the manganese(II) enzyme in the hydrolysis of p-nitrophenyl acetate revealed an inflection point at pK = 8.2. The hydration number of manganese(II) carbonic anhydrase could be derived using either the frequency dependence of T1p or the T1p/T2p ratio at only one (high) frequency. Both treatments are in agreement with a model in which one water molecule is bound to the metal at high pH. At low pH the relaxation data imply that no-H20 exists in the first coordination sphere of the manganese ion. The various parameters which are responsible for the proton relaxation mechanisms have been evaluated and are compared to other manganese(II) enzyme systems. The pH dependence of the binding constant of manganese to apocarbonic anhydrase is also reported.

Animals↗