Biomedical subjects

A Niles

Publications and source records attributed to A Niles.

4 recordsLinked to original sources

PubMed2005

Temperature determination using Kalpha spectra from M -shell Ti ions.

The compact multipulse terawatt (COMET) laser facility at LLNL was used to irradiate Al-coated 2-50 microm Ti foils with approximately 10(19) W cm(-2) , 500 fs, 3-6 J laser pulses. Laser-plasma interactions on the front side of the target generate hot electrons with sufficient energy to excite inner-shell electrons in Ti, creating Kalpha emission which has been measured using a focusing spectrometer with spatial resolution aimed at the back surface of the targets. The spatial extent of the emission varies with target thickness. The high spectral resolution (lambda/Deltalambda approximately equal to 3800) is sufficient to measure broadening of the Kalpha emission feature due to the emergence of blueshifted satellites from ionized Ti in a heated region of the target. A self-consistent-field model is used to spectroscopically diagnose thermal electron temperatures up to 40 eV in the strongly coupled Ti plasmas.

Journal Article↗

PubMed2001

Definition of the extended substrate specificity determinants for beta-tryptases I and II.

Tryptases betaI and betaII were heterologously expressed and purified in yeast to functionally characterize the substrate specificity of each enzyme. Three positional scanning combinatorial tetrapeptide substrate libraries were used to determine the primary and extended substrate specificity of the proteases. Both enzymes have a strict primary preference for cleavage after the basic amino acids, lysine and arginine, with only a slight preference for lysine over arginine. betaI and betaII tryptase share similar extended substrate specificity, with preference for proline at P4, preference for arginine or lysine at P3, and P2 showing a slight preference for asparagine. Measurement of kinetic constants with multiple substrates designed for beta-tryptases reveal that selectivity is highly dependent on ground state substrate binding. Coupled with the functional determinants, structural determinants of tryptase substrate specificity were identified. Molecular docking of the preferred substrate sequence to the three-dimensional tetrameric tryptase structure reveals a novel extended substrate binding mode that involves interactions from two adjacent protomers, including P4 Thr-96', P3 Asp-60B' and Glu-217, and P1 Asp-189. Based on the determined substrate information, a mechanism-based tetrapeptide-chloromethylketone inhibitor was designed and shown to be a potent tryptase inhibitor. Finally, the cleavage sites of several physiologically relevant substrates of beta-tryptases show consistency with the specificity data presented here.

Humans↗

PubMed1991

Collaborative feasibility study of a biphasic system (Roche Septi-Chek AFB) for rapid detection and isolation of mycobacteria.

A study to delineate the feasibility of a biphasic-culture approach for detection and isolation of mycobacteria from clinical specimens except blood was conducted in four medical centers. The biphasic system (Septi-Chek AFB, Roche Diagnostic Systems, Nutley, N.J.) was compared with conventional mycobacterial isolation media and the BACTEC system. Septi-Chek AFB showed the highest degree of mycobacterial recovery. In addition, Septi-Chek AFB consistently shortened the time required for recovery of mycobacteria from clinical specimens and supported the growth of small inoculum numbers of stock cultures of 14 mycobacterial species. The study indicates the feasibility and potential advantages of the biphasic approach for detection and isolation of mycobacteria.

Bacteriological Techniques↗

PubMed1984

Evaluation of the Quantum II and Rapid E identification systems.

A total of 492 clinical isolates from the family Enterobacteriaceae were tested in the API 20E, Rapid E, and Quantum II identification systems. Discrepant identifications among these three systems were resolved by repeat testing in the identification systems or use of conventional biochemical tests. Of these isolates, 94.1% were correctly identified with the API 20E and Rapid E systems, and 97.0% were correctly identified with the Quantum II system. An additional 48 non-Enterobacteriaceae isolates were tested with the Quantum II system, and 83.3% were correctly identified. The majority of incorrect identifications with the Rapid E and Quantum II systems were caused by a single aberrant biochemical reaction. Reproducibility of the biochemical reactions obtained with these two systems was evaluated by testing 40 organisms in triplicate. Identical biocodes for all three tests were obtained for 10 organisms with the Quantum II system and for 19 organisms with the Rapid E system. Reproducibility of the Quantum II test results was improved with a subsequent modification of the photometer of this system. Both the Rapid E and Quantum II systems were inexpensive and were technically easy to inoculate and interpret.

Bacteriological Techniques↗