Biomedical subjects

R de Beer

Publications and source records attributed to R de Beer.

21 records · Page 2Linked to original sources

PubMed1980

The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure.

The g-value and linewidth of ESR spectra of methylamine dehydrogenase (primary-amine:(acceptor) oxidoreductase (deaminating) EC 1.4.99.-) and methanol dehydrogenase (alcohol:(acceptor) oxidoreductase, EC 1.1.99.8) are very similar. This similarity is also reflected in electron-nuclear double resonance (ENDOR) results, the coupling constants of two protons in one enzyme equalling those in the other. The presence of a third proton in the ENDOR spectrum of methylamine dehydrogenase suggests a different structure or a different kind of interaction which can be related to the finding that the resolved ROSTHETIC GROUP IS PROTEIN-BOUND. The bound prosthetic group has a high redox-potential, supporting the conclusion from the ESR and ENDOR results that it is a quinone derivative.

Electron Spin Resonance Spectroscopy↗

PubMedDate not supplied

Application of time-domain fitting in the quantification of in vivo 1H spectroscopic imaging data sets.

Time-domain model function fitting techniques were applied to improve the reconstruction of metabolite maps from the data sets obtained from in vivo 1H spectroscopic imaging (SI) experiments. First, residual water-related signals were removed from the SI data sets by using SVD-based linear time-domain fitting based upon the HSVD (State Space) approach. Second, peak integrals of the metabolites of interest were obtained by quantifying the proton spin-echoes of the voxels by means of non-linear time-domain fitting based upon the maximum likelihood principle. Third, in order to save computational time, interpolation of the metabolite images (from size 32 x 32 to 128 x 128) was performed in the image-domain by applying one-dimensional cubic splines. It was found that the residual water signals can be almost completely removed from the SI data sets by applying the linear HSVD fitting method. Furthermore, it was found that voxel dependency of certain NMR parameters (e.g., variations of the spin-echo offset frequencies and/or phase factors) can be accounted for automatically by applying the nonlinear time-domain fitting technique. For that purpose it appeared to be essential to employ prior knowledge of the NMR spectral parameters.

Aspartic Acid↗

PubMedDate not supplied

Evaluation of five protocols for quantification of two-dimensional MR spectroscopic images.

Five protocols were tested for quantification on in vivo two-dimensional spectroscopic imaging datasets. The datasets are duplo measurements from three individuals. The peaks for N-acetyl aspartate, creatines, and cholines were quantified. The first of the protocols is conventional integration of a selected interval around the peak. The others are various implementations of a Gauss-Newton-based least-squares time-domain fitting algorithm. Fitting a half-echo (free-induction decay curve, FID) to a full echo was compared; this was combined with or without filtering out the water signal using the Lanczos-Hankel singular-value decomposition (LHSVD). It appears that conventional integration yields consistent and accurate results in comparison to the fitting methods. The combination of LHSVD and echo fitting performs equally well; advantages and disadvantages are discussed. The protocols using FID fitting perform poorly with these experimental datasets.

Adult↗