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Biomedical subjects

G Weimann

Publications and source records attributed to G Weimann.

At least 19 recordsLinked to original sources

Stroke: evaluation of long-term rehabilitation effects.

A planned prospective documentation of the course of rehabilitation of 303 stroke patients was undertaken using the Bathel-Index as a measure of basic everyday functions and the Guttman-Scale as a measure of complex activities of daily living. These were determined at the beginning of rehabilitation, after an average of 7 weeks of in-patient treatment and one year following the stroke. Four patterns in the course of rehabilitation could be differentiated. The causes of the differing functional results were investigated. Besides a positive spontaneous progress of the underlaying disease with an early reparation of the neurological deficits it is the premorbid status, the overprotection of the physically disabled and the determinative cognitive and mental functions that decide the long term fate of stroke patients.

Activities of Daily Living

Structure of lactate dehydrogenase inhibitor generated from coenzyme.

Two inhibitors of lactate dehydrogenase generated during NADH storage have been isolated by chromatography. One is a dimer of the dinucleotide where the AMP moiety is unmodified. The other is also generated from NAD+ in the presence of a high concentration of phosphate ions at alkaline pH. This inhibitor was proved to be the addition compound of one phosphate group to position C-4 of the nicotinamide ring of NAD+ by NMR spectroscopy, enzymatic cleavage, and dissociation to NAD+ at neutral pH. This compound is a competitive inhibitor with respect to NAD+ in the presence of the lactate dehydrogenase with a Ki of 2 X 10(-7) M. The interaction of this inhibitor with lactate dehydrogenase is discussed relative to the structure of this enzyme.

Alkaline Phosphatase

[Tetany].

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Calcium

X-ray study of the lithium complex of NAD.

The Li+-NAD+ complex exists as a 'dimer' of two molecules arranged head-to-tail with Li+ coordinated tetrahedrally to adenine N(7) and three pyrophosphate oxygens. Adenine is stacked intermolecularly on nicotinamide. The conformation of NAD+ is 'extended' and similar to that found in holoenzyme complexes. This is in contrast to the 'folded' structure proposed from spectroscopic studies.

Cations, Monovalent