Bernstein modes in quantum wires and dots.
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Biomedical subjects
Publications and source records attributed to B Meurer.
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Dynamics of tetrapropylammonium (TPA) cation occluded during the synthesis in a siliceous MFI zeolite is investigated by 1H broad-line nuclear magnetic resonance (NMR) methods. Second moments M2, spin-lattice relaxation times T1 and T1 rho are measured in a large temperature domain. To al comparison, similar measurements are also reported in bulk tetrapropylammonium bromide (TPABr). Whereas methyl reorientation at low temperature and tumbling of the cation in the plastic phase are observed in crystalline TPABr in accordance with published studies, a new slower motion which could not be identified is observed below the phase transition. Such a motion is much more clearly shown by the existence of a minimum of T1 rho in a quenched sample. Our measurements in the zeolite demonstrate that the TPA template exhibits a larger and more complex mobility below 378 K. Beyond the fast methyl reorientation, the results disclose a motion which probably involves the entire propyl arms inside the channels. So the zeolite framework seems to make such a kind of motion easier. On the contrary, even at 450 K, the highest temperature investigated, the tumbling which would necessitate exchange of the propyl arms between the channels is not observed. A slow motion, responsible for a decrease of T1 rho above 350 K, could not be identified. While a simple correlation time is sufficient to describe the relaxation time dependences in TPABr, a distribution (such as Williams-Watts) is required to account for those in the zeolite.
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The authors relate the findings in the 1H solid state line shape (at 60 MHz) of human aortic walls (n = 12) in native state and after histologically controlled selective lysis of collagen and elastin. An analysis of the line shape shows a composite free induction decay (FID) consisting of a low amplitude (3-7%) fast decaying component (T2 approximately 20 microseconds) and a slow decaying one (T2 > 1 ms). The fast component is identified as the protons of the collagen macromolecules. The second moment computed from the experimental fast component of the FID is in agreement with published studies examining the motional characteristics of collagen by multinuclear NMR employing spin labeling. A theoretical second moment is computed for the collagen macromolecular backbone from the atomic positions in the superhelix. Comparison with the observed experimental values allows determination of the step angle (29 degrees) of the fast rotational motion of the collagen strands along their long axis.
The elasticity of the human aortic wall in longitudinal uniaxial elongation at high strain, known to be determined mostly from tissular collagen's behaviour, is studied and compared to the second moment of the 1H nuclear magnetic resonance (NMR) solid state line-shape, a proton nuclear magnetic resonance (at 60 MHz) characteristic for the molecular motion and the rigidity of the collagen macromolecular backbone. The 1H NMR signal of collagen is identified after selective histologically controlled chemical lysis. The computed second moment of the line-shape shows statistically significant correlation with the slope of the strain-stress curve of the aorta at high strain, thus proving the relationship between a macroscopic tissular elasticity parameter and a macromolecular rigidity characteristic of collagen, a major tissular component. In vivo extension of this technique (e.g., MRI) would allow us to gain information on the biomechanical state of the aorta, a naturally highly stressed and strained tissue.
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OBJECTIVES AND RATIONALE: Previous studies have suggested a relationship between tissue magnetic resonance (MR) relaxation times and its biomechanical behavior. To further investigate this relationship, the authors studied 41 human vascular wall samples from different anatomic localizations, including systemic and pulmonary arterial, as well as venous tissues. METHODS: The authors measured water content, proton MR T1 and T2 relaxation times, and two viscoelastic parameters of the samples at 4 MHz. RESULTS: T2, water content, and both viscoelastic variables significantly differed among the five anatomic localizations (P less than .05). Both T1 and T2 were significantly (P less than .05) and linearly related to viscoelastic parameters. Multiple linear regression showed that both viscoelastic parameters of a sample can be predicted from the measured values of T1 and T2. CONCLUSIONS: These results provide a basis for characterizing the mechanical stress of a tissue by knowing its MR relaxation times.
Three enolase isoenzymes can be distinguished after electrophoresis of yeast crude extracts. After adding glucose to derepressed cells, there was a coordinated increase in the activity of enolase I and decrease in enolase II activity. Enolase I was found to be repressed and enolase II simultaneously induced by glucose. The third enolase activity remained unchanged and was identified as that of a hybrid enzyme. Enolase catalyses the first common step of glycolysis and gluconeogenesis. Gluconeogenic enolase I shows substrate inhibition for 2-phosphoglycerate (glycolytic substrate) and glycolytic enolase II is substrate-inhibited by phosphoenolpyruvate (gluconeogenic substrate). The gluconeogenic reaction was inhibited up to 45% by physiological concentrations of fructose 1,6-bisphosphate. To test for cytological compartmentation, a method was developed for isolating microsomes. Effective enrichment of rough and smooth endoplasmic reticulum was demonstrated by electron microscopy. No evidence was obtained for any compartmentation of either enolases or other glycolytic enzymes.
A method for the rapid isolation of yeast enolases, yielding three distinct isoenzymes, has been devised. In the first step anionic proteins were precipitated with polyethyleneimine, whereas hydrophobic enolase isoenzymes remained in the supernatant. Secondly, the supernatant was 45% saturated with ammonium sulfate and bound to phenyl-Sepharose CL-4B. Decreasing ammonium sulfate and simultaneously increasing ethylene glycol concentrations were used for elution. Finally, enolase isoenzymes were separated by chromatofocusing. The purified isoenzymes gave single bands after isoelectric focusing.
Mn2+ binding to poly(acrylic acid) at different degrees of ionization, alpha, has been studied from the frequency dependence of the water protons' relaxation rates T1(-1) and T2(-1). Site binding is treated as an equilibrium with the concentration of free ions at the immediate vicinity (CIV) of the polyion. The CIV is calculated as the solution of the Poisson-Boltzmann equation at the surface of the cylindrical polyion. A single value of K is shown to fit the results at all values of alpha. The amount of site binding is higher than the total amount of condensed divalent counterions predicted for a finite polyion concentration in the presence of monovalent counterions by Manning's theory.
Chemical shift and relaxation time measurements on the water protons in polyelectrolyte solutions containing divalent paramagnetic counterions have shown the existence of three types of counterions: - site bound with loss of water molecules and partial or complete release of the electrostriction in the first hydration sphere, - atmospherically trapped with no change in hydration, - free. The overall stoichiometry of the two former is in agreement with Manning's fraction of condensed counterions. A complete analysis of the frequency dependent contribution of site bound counterions to the water protons relaxation times leads us to interesting conclusions on the modifications of the first hydration shell and on the life time of site binding.
Collagen is a major component of the extracellular matrix and a determinant of the elastic behavior of the human aorta. To investigate the changes found in aneurysmal degeneration, the authors studied the solid-state hydrogen-1 nuclear magnetic resonance line shape of collagen in aneurysms and normal human aortas. A three-component decomposition of the free induction decay was performed, with collagen characterized by a T2 of about 18 microseconds. The second moment of the collagen line shape was found to be increased in aneurysms (5.3 vs 4.8 G2), while, correspondingly, the T2 of collagen was lower in aneurysms (16.3 vs 17.7 microseconds). This corresponds to a modification of collagen structure and molecular motion. Collagen concentration was lower in nondiseased aortic walls (9.4% vs 7.3%). These results are discussed in reference to the contradictory conclusions in the current literature. The increase in collagen and the modification of its structure and molecular motion are explained by the need to resist an increasing tangential tension due to increased aortic diameter and diminished wall thickness in aneurysms and by intercalation or site binding in the helices or electric dipolar interactions in the less mobile side groups.