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Biomedical subjects

D H Russel

Publications and source records attributed to D H Russel.

4 recordsLinked to original sources
PubMed1989

Phase synchronization of an ion ensemble by frequency sweep excitation in Fourier transform ion cyclotron resonance.

The Fourier transform ion cyclotron resonance (FT-ICR) signal is produced by the coherent motion of a population of ions. The ability to produce a well-defined ion packet by excitation of an initially random ion ensemble is a major limiting factor of high mass FT-ICR. Ions must be both resonant and in phase with the applied radio frequency excitation field to be accelerated to radii suitable for detection by FT-ICR. Synchronization of the phase angles of an ensemble of ions occurs by off-resonant acceleration during frequency swept excitation. Results from computer-simulated ion trajectories suggest that phase synchronization of the ion packet prior to resonant excitation results in better spatial definition of the ion ensemble.

Computer Simulation↗
PubMed1977

Ornithine decarboxylase may function as an initiation factor for RNA polymerase I.

Reparts suggest that the activity of RNA polymerase I is modulated by a labile protein with a hlaf-life of 10 to 20 minutes. Ornithine decarboxylase is the only labile protein (half-life, 10 to 20 minutes) that increases in activity prior to increased RNA polymerase I activity. The addition of a small amount of a highly purified ornithine decarboxylase preparation to an RNA polymerase I assay increases the initial rate of the reaction as well as the time for which the assay is linear. The incorporation patterns of 14C-labeled adenosine triphosphate and 32P-labeled adenosine triphosphate into RNA indicate that the addition of ornithine decarboxylase to the RNA polymerase assay increases the rate of initiation. This report demonstrates a novel way to purify ornithine decarboxylase by RNA polymerase I affinity chromatography and presents data in support of the hypothesis that the labile protein which modulates RNA polymerase I activity is ornithine decarboxylase.

Animals↗
PubMedDate not supplied

Induction of ornithine decarboxylase in Reuber H35 rat hepatoma cells.

Stimuli known to induce tyrosine aminotransferase in H35 cells were tested relative to their ability to induce ornithine decarboxylase, the initial enzyme in the polyamine biosynthetic pathway. Dibutyryl cyclic AMP (0.5 mM), parachlorophenylthio-cyclic AMP (0.1 mM) and dexamethasone (1 muM) stimulated the activity of ornithine decarboxylase 7- to 8-fold by 5 hr of induction. There was a delay of 1 hr before any increase in enzyme activity was detectable. Insulin administered alone failed to significantly change ornithine decarboxylase activity. The ability of dibutyryl cyclic AMP to elevate ornithine decarboxylase activity was found to be concentration-dependent, and a dose-response relationship very similar to that for the induction of tyrosine aminotransferase by dibutyryl cyclic AMP was observed in these cells. The ability of various 8-substituted cyclic AMP analogues to increase the activity of ornithine decarboxylase was correlated with their ability to activate purified protein kinase.

Animals↗