Public and private health insurance in Germany: the ignored risk selection problem.

We investigate risk selection between public and private health insurance in Germany. With risk-rated premiums in the private system and community-rated premiums in the public system, advantageous selection in favor of private insurers is expected. Using 2000 to 2007 data from the German Socio-Economic Panel Study (SOEP), we find such selection.

Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida.

D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases/reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida, which was recombinantly expressed in Escherichia coli, in three different crystal forms to resolutions between 1.9 and 2.

Molecular basis of substrate recognition in D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida.

D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida (EC 1.1.1.

Development of a decision support model for scheduling clinical studies and assigning medical personnel.

Clinical studies for the development of new drugs in the pharmaceutical industry consist of a number of individual tasks which have to be carried out in a pre-defined chronological order. Each task requires certain types of medical personnel. This paper investigates the scheduling of clinical studies to be performed during a short-term planning horizon, the allocation of workforce between the studies, and the assignment of individual employees to tasks.

Nano-electrospray mass spectrometry with a modified commercial IonSpray source.

Electrospray mass spectrometry is a standard tool for the investigation of biological samples. Due to the high flowrates of the standard sources, large sample amounts are required and it is almost impossible to spray physiological solutions due to their aqueous medium. The introduction of microelectrospray sources has made it possible to decrease the sample amounts needed and enabled the use of buffered solutions.

[Not Available].

A method for the combined extraction of the mycotoxins aflatoxin B1, B2, G1, G2, ochratoxin A (OTA) und zearalenone (ZEA) in cereals is described. After extraction with acetonitril/water a clean-up for the mycotoxins was made using solid-phase columns (SiOH) or a combination of two immunoaffinity columns (aflaochra- and zearala-test-column from Vicam). The aflatoxins, ochratoxin A and zearalenone were detected after pre-column derivatization with trifluoroacetic acid in one HPLC run.

A general ribonuclease assay using methylene blue.

Ribonuclease (RNase) activity has been assayed by monitoring the shift in the absorbance maximum of methylene blue upon intercalation into high-molecular-weight RNA. After preincubation of yeast RNA with methylene blue, the initial rate of hydrolysis can be followed spectrophotometrically at a wavelength of 688 nm. This allows enzyme kinetic studies of RNases with their probable native substrate, RNA, in place of the artificial ones, such as dinucleoside phosphates or cyclic monophosphates, currently used.

Purification of pro- and eukaryotic superoxide dismutases by charge-controlled hydrophobic chromatography.

The process of purifying superoxide dismutases was simplified using charge-controlled hydrophobic chromatography on 10-carboxydecyl Sepharose. In only one chromatographic step following ammonium sulphate precipitation, Fe-containing superoxide dismutase from Pseudomonas putida and Cu,Zn-containing superoxide dismutase from bovine erythrocytes were purified with an overall yield of about 70% to electrophoretic homogeneity. The specific activities of the crystalline enzyme preparations were expressed in McCord and Fridovich units and were 3000 and 3200 U/mg, respectively.

[Determination of the activity of superoxide dismutase in terms of rea substrate conversion].

On the basis of photochemical generation of O2.- and the tetrazolium/formazan system as indicating reaction an assay for SOD was developed which allows the determination of initial rate velocities of the enzyme. This was achieved by a special apparatus yielding the continuous registration of product formation simultaneously with the photochemical generation of O2.

[Purification and various properties of NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus].

The constitutive NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus can be accumulated about 50 fold in 3 purification steps. The end-product shows in the analytical polyacrylamide gel electrophoresis only one active enzyme band. The molecular weight of the enzyme was determined to be 235,000 by gel chromatography on Sephadex G 200, the smallest subunit shows a molecular weight of 61 000 on SDS electrophoresis.