Evaluation of recombinant enzyme calibration to harmonize lipoprotein-associated phospholipase A2 activity results between instruments.

Objectives: Enzymatic activity of lipoprotein-associated phospholipase A2 (Lp-PLA2) mediates vascular inflammation in coronary heart disease (CHD). Calibration of Lp-PLA2 activity measurements using a recombinant enzyme was performed to assess intra- and inter-laboratory assay precision and accuracy in routine clinical settings.

Design And Methods: Test performance assessment included recovery, analytical sensitivity, linear range, within-lab and site-to-site precision, interference, and analyte stability.

Photo-cross-linkable oligonucleotide probes for in situ hybridization assays.

In situ hybridization techniques have been an important research tool since first introduced 30 years ago, and more recently clinical applications have been expanding greatly. Still, further improvements in the assay sensitivity and protocols that are amenable to routine clinical use are desired. We use a novel photo-cross-linking technology to irreversibly bind short oligonucleotide probes to the target sequence following a hybridization period.

Identification and characterization of allergens in two species of tuna fish.

Background: In countries where fish consumption is high, allergenic reactions to fish are common among patients diagnosed with food hypersensitivity. For tuna fish, allergenic proteins are not known. In addition, it is not known how the tuna fish extracts should be processed to obtain optimal in vitro diagnostic performance and to preserve labile antigens.

Capacity of Helicobacter pylori to generate ionic gradients at low pH is similar to that of bacteria which grow under strongly acidic conditions.

Helicobacter pylori colonized the highly acidic human gastric mucosa. At pH 3.0 to 7.

Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival.

Starvation proteins synthesized by Escherichia coli at the onset of carbon starvation (R. G. Groat and A.