Fully Automated Forensic Routine Dried Blood Spot Screening for Workplace Testing.

In this study, we describe the transfer of a new and fully automated workflow for the cost-effective drug screening of large populations based on the dried blood spot (DBS) technology. The method was installed at a routine poison control center and applied for DBS and dried urine spot (DUS) samples. A fast method focusing on the high-interest drugs and an extended screening method were developed on the automated platform.

Extended and Fully Automated Newborn Screening Method for Mass Spectrometry Detection.

A new and fully automated newborn screening method for mass spectrometry was introduced in this paper. Pathological relevant amino acids, acylcarnitines, and certain steroids are detected within 4 min per sample. Each sample is treated in an automated and standardized workflow, where a mixture of deuterated internal standards is sprayed onto the sample before extraction.

Mass spectrometry-assisted protease substrate screening.

Since sequencing of the human genome was completed, more than 500 genes have been annotated as proteases. Exploring the physiological role of each protease requires the identification of their natural substrates. However, the endogenous substrates of many of the human proteases are as yet unknown.

Renal cathepsin G and angiotensin II generation.

Background: Alternative pathways of angiotensin II biosynthesis play a significant role in the renin-angiotensin system. In this study porcine renal tissue was investigated for angiotensin II-generating enzymes.

Methods And Results: Protein extracts from porcine renal tissue were fractionated by liquid chromatography and tested for their angiotensin II-generating activity by the mass-spectrometry-assisted enzyme screening system (MES) and the active fractions were purified to near homogeneity.

Principle and applications of the protein-purification-parameter screening system.

For the purification of a target protein, liquid chromatography is the method of choice, if its activity has to be maintained. The selection of optimum parameters will improve in proportion to the number of individual parameters varied in initial experiments. Here a fast screening method is described, which utilizes automated parallel chromatographic experiments in the batch mode in 96-well plates.

Detection of protease activities with the mass-spectrometry-assisted enzyme-screening (MES) system.

The MALDI-MES provides a rapid, sensitive and reproducible alternative approach to existing analytical techniques for the detection of enzymatic activities that does not require a chromophore or radiolabeling. An improved method is presented, by which enzymes with defined substrate specificities can be detected with a MALDI mass spectrometer in complex protein fractions. In order to demonstrate the utility of the new method, in this study we describe the use of MALDI-MES to detect proteolytic activities in a protein extract from porcine renal tissue, which contained several thousand proteins as visualized by 2D electrophoresis.