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Biomedical subjects

R Kimmich

Publications and source records attributed to R Kimmich.

At least 55 records · Page 3Linked to original sources

Motion-insensitive volume-selective pulse sequences for direct and proton-detected 13C spectroscopy: detection of glycogen in the human liver in vivo.

Two compact pulse sequences are reported for the volume-selective detection of 13C nuclei. 13C signals are either directly acquired after enhancing the amplitude by polarization transfer from the coupled protons or, preferably, indirectly detected by heteronuclear editing of proton signals of 1H nuclei coupled to 13C. In the latter case, the full sensitivity of proton resonance is achieved, and signals from uncoupled protons or protons coupled to non-13C nuclei or 13C nuclei of undesired compounds are suppressed. Both sequences are single-scan procedures and are insensitive to the pulse phases and to motions of the investigated organs. The insensitivity to organ motions is due to the extremely compact character of these sequences avoiding coherence evolution periods as far as possible. This is achieved first by the introduction of double-resonance sandwich (DORSA) pulses accomplishing the polarization transfer slice selectively in a very short time. The second reason is that the initial evolution interval which is usually part of polarization transfer experiments is avoided by the aid of a doublet line-selective inversion pulse. Several test experiments in vivo are reported. In particular, it is demonstrated that glycogen can be detected in natural abundance in the human liver in vivo using a 2-T whole-body tomograph even without the use of heart or respiration triggers. The total acquisition time was 22 min, and a signal-to-noise ratio of 6 was achieved.

Carbon↗

Hydrogen/fluorine retuning tomography. Applications to 1H image-guided volume-selective 19F spectroscopy and relaxometry of perfluorocarbon emulsions in tissue.

A hardware modification which permits the record of 19F images, spectra, and relaxation times with a 1H tomography bird-cager resonator is described. Changing the spectrometer frequency from 1H to 19F resonance and vice versa is possible without removing the object to be investigated. This hydrogen/fluorine retuning tomography (HYFY) technique permits studies of identical slices or volume elements with 1H as well as with 19F resonance. In particular, it is possible to localize volume elements on the basis of multislice proton images and then to investigate these volume elements with fluorine magnetic resonance by the aid of volume selection methods. For this purpose, pulse sequences for the localized and spectroscopically resolved determination of spin-lattice and transverse relaxation times have been developed. The applicability of the techniques has been demonstrated by the aid of phantom samples as well as with excised porcine organs which have been perfused with perfluorocarbon emulsions.

Connective Tissue↗

Volume-selective and spectroscopically resolved NMR investigation of diffusion and relaxation in fertilised hen eggs.

A radiofrequency and field-gradient pulse sequence is presented permitting the non-invasive, volume-selective and spectroscopically resolved determination of incoherent transport parameters with the aid of an NMR field-gradient method. With proton NMR, diffusion or (quasi-incoherent) perfusion coefficients as low as 10(-12) m2 s-1 are accessible with gradients G less than or equal to 100 mT m-1 for T2 greater than or equal to 0.3 s. If coherent motions like flow are superimposed, the gradient pulses can be compensated for phase shifts arising from uniform or accelerated motions. The efficiency of the suppression of the influence of coherent motions was demonstrated in test experiments with phantom sample arrangements. As a biophysical application, the local diffusion coefficients D and relaxation times T1 and T2 of hen eggs were studied during the first days of incubation. In the yolk, strongly non-exponential decay curves were observed for the CH2 line. The translational displacements of water were found to be restricted. The relaxation and diffusion parameters turned out to be constant during the incubation. Medical applications of the pulse sequences are discussed. In one case we demonstrate that attempts to assign resonance lines can be checked by the condition that resonances of the same compound must have identical diffusion coefficients.

Animals↗

Single-scan volume-selective spectral editing by homonuclear polarization transfer.

An RF and field gradient pulse sequence is presented permitting the single-scan volume-selective spectral editing of the signals of coupled spins. The attribute "single scan" means that the editing of resonance lines is performed in each accumulation or phase cycling scan rather than by subtraction of independently acquired signals. As an example the methyl line of lactate has been investigated. The method is considered to be a useful tool in biomedical research using lactate as an ischemic parameter. The basic principles applied are the VOSY pulse scheme for volume selection and the INEPT sequence for homonuclear polarization transfer from the CH to the CH3 groups. As an intrinsically single-scan editing method ("homonuclear single-scan VOSING procedure"), the pulse train is expected to provide results that are more reliable than the two-scan subtraction methods previously reported.

Lactates↗

Double-quantum filtered volume-selective NMR spectroscopy.

An RF and field-gradient pulse sequence is presented, permitting the recording of localized double-quantum filtered proton spectra. In this way distinction between overlapping resonances of coupled and uncoupled spins is possible. The editing of the lactate methyl line is demonstrated in a test experiment.

Magnetic Resonance Spectroscopy↗

Single-scan volume-selective editing of NMR spectra with the aid of a split-pathway technique for homonuclear applications.

An RF and field-gradient pulse sequence that permits the recording of localized and edited proton spectra is presented. The editing principle is a technique of splitting and recombining the coherence pathways. While the recombination of the pathways of uncoupled spins is destructive, that of coupled spins can be adjusted to be constructive.

Magnetic Resonance Spectroscopy↗

Volume-selective determination of the spin-lattice relaxation time in the rotating frame T1 rho, and T1 rho imaging.

A method for the volume- and resonance line-selective determination of the longitudinal relaxation time in the rotating frame, T1 rho, is described. The spin-lock pulse intrinsic to the T1 rho sequence simultaneously replaces the first slice-selective pulse of the VOSY method for localized spectroscopy. This is a further parameter suitable for the local characterization of tissue. On the same basis, T1 rho can be used as a new contrast parameter for biomedical imaging purposes. An appropriate pulse sequence for T1 rho imaging is presented. Test experiments which promise some striking advantages compared with conventional magnetic resonance imaging are reported.

Animals↗

T1 rho dispersion imaging and volume-selective T1 rho dispersion weighted NMR spectroscopy.

Pulse sequences which permit imaging and volume-selective determination of parameters characterizing the frequency dependence of the spin-lattice relaxation time in the rotating frame, T1 rho, are presented. The contrasts are due to slowly moving macromolecules or paramagnetic contrast agents. In vivo test experiments were carried out with tumorous mice treated with a contrast agent. It is shown that the contrast effect is dramatically enhanced in T1 rho dispersion images compared with images weighted by any of the relaxation times.

Animals↗

Integrated volume-selective/spectral editing 1H NMR and postdetection signal processing for the sensitive determination of lactate.

A new volume selection/spectral editing pulse sequence (VOSING) is presented. The features specific to the technique are that the volume selection and the editing intervals coincide and that no decoupling is necessary. The pulse sequence can be applied under both homo- and heteronuclear conditions. Phantom experiments with lactate solutions and human serum led to water suppression factors of about 20,000. A postdetection signal processing method has been implemented. The final sensitivity for lactate determinations could thus be improved by a factor of more than 4. Ischemia-induced lactate could easily be detected in serum. At present, the lower detection limit of lactate is 1 mmol/liter for a (1.2 cm)3 voxel and 32 scans in a 4.7-T/40-cm magnet.

Humans↗

Deuteron field-cycling relaxation spectroscopy and translational water diffusion in protein hydration shells.

The deuterated hydration shells of bovine serum (BSA) albumin, and purple membrane sheets have been studied by the aid of deuteron field-cycling relaxation spectroscopy. The deuteron Larmor frequency range was 10(3) to 10(8) Hz. The temperature and the water content has been varied. The data distinguish translational diffusion on the protein surface from macromolecular tumbling or exchange with free water. A theory well describing all dependences has been developed on this basis. All parameters have successfully been tested concerning consistency with other sources of information. The concept is considered as a major relaxation scheme determining, apart from cross-relaxation effects, the water proton relaxation in tissue.

Biophysical Phenomena↗

Volume-selective multi-pulse spin-echo spectroscopy and selective suppression of spectral lines.

A method is described allowing the recording of in vivo NMR spectra in sharply bound volume elements preselected on the basis of slice images. Experiments with phantom samples, as well as with a test person in a whole-body instrument, have been carried out to demonstrate the applicability of the technique. In the case of proton spectroscopy, suppression of the water and/or or of the lipid line is often desirable. A corresponding pulse sequence has been implemented and successfully tested with a phantom sample.

Humans↗

14N1H and 2H1H cross-relaxation in hydrated proteins.

The frequency dependence of the proton spin-lattice relaxation time T1 of solid hydrated bovine serum albumin and alpha-chymotrypsin has been measured over 4.5 decades in the range 10(4) to 3 X 10(8) Hz mainly by the aid of the field-cycling technique. The comparison between H2O- and D2O-hydrated samples permitted the distinction of exchangeable and unexchangeable protons. In all cases the 14N1H cross-relaxation dips due mainly to the amide groups have been observed. In addition, in the case of the deuterium exchanged proteins a 2H1H quadrupole dip appears. The amide groups act as relaxation sinks due to the coupling of the amide proton to 14N and adjacent protons. Outside of the dip regions the proton-proton coupling dominates. The fluctuations of the 14N1H and 1H1H interactions are of a different type. The unexchangeable protons show a T1 dispersion outside of the quadrupole dip regions given by the exceptional power law T1 approximately v0.75 +/- 0.05. It is shown that apart from structural information of the 14N spectra, 14N1H cross-relaxation spectroscopy permits the determination of correlation times in the range 10(-7) s less than tau less than 10(-4)S.

Animals↗

Characterization of the mobility of various chemical groups in the purple membrane of Halobacterium halobium by 13C, 31P and 2H solid state NMR.

Lyophilized purple membrane sheets have been investigated by C-13- and P-31-cross polarization/magic angle spinning NMR spectroscopy. The high-resolution C-13 spectrum and its non-quaternary suppression version indicate fast protein side-chain motions but a rigid backbone structure on a time scale of roughly less than 0.001 to 0.01 s. Three components of exchangeable hydrogen have been detected by deuterium NMR. The mean exchange time of the peptide hydrogens must be longer than 1 microsecond. The medium component is attributed to mobile side-chains. In addition a narrow line has been observed which is assigned to the residual hydration water.

Bacteriorhodopsins↗

NMR field-cycling relaxation spectroscopy of bovine serum albumin, muscle tissue, Micrococcus luteus and yeast. 14N1H-quadrupole dips.

The frequency dependence of the proton spin lattice relaxation time of bovine serum albumin, muscle tissue, Micrococcus luteus and yeast has been measured by the aid of the field-cycling technique. In all systems 14N1H-quadrupole dips have been observed. The conclusion is that amide groups are the dominating relaxation centers up to approx. 10(7) Hz. This finding can be understood by the fact that protein backbone fluctuations and, if possible, tumbling of the whole molecule rather than side group motions are the relevant mechanisms in this frequency range. A proton relaxation scheme for cells and tissue is presented.

Animals↗

Solvation of oxygen in lecithin bilayers.

The solubility of oxygen in dipalmitoyllecithin (DPL) and paraffinc C19 has been investigated by measurement of the enhanced proton relaxation rates under the influence of oxygen pressure. The paraffin shows a noticeable effect in the rotator phase, but not so in the crystalline phase. tin contrast to paraffins, both phases of DPL-bilayers dissolve oxygen, but the solubility in the liquid-crystalline phase is greater than in the crystalline state by a factor approximately equal to 3. Furthermore, the experiments indicate a distribution of electron relaxation times in the crystalline phase in contrast to the liquid-crystalline phase. A possible explanation of this behaviour is a multiphase structure of the "crystalline' lamellae. The biological relevance of thbse results could be a triggering of the gas-transport by the alveolar lining of lungs, if cyclic phase transitions occur during the breathing-cycle.

Binding Sites↗