Biomedical subjects

M Böhmer

Publications and source records attributed to M Böhmer.

8 recordsLinked to original sources

PubMed2001

Novel diode laser-compatible fluorophores and their application to single molecule detection, protein labeling and fluorescence resonance energy transfer immunoassay.

We describe a series of new long-wave absorbing and fluorescing cyanine dyes and labels (based on a general logic for the design of such dyes), their spectra, covalent and noncovalent linkage to proteins, their use in single molecule detection (SMD) and as donors and acceptors, respectively, in fluorescence resonance energy transfer studies. The new labels represent water-soluble and reactive fluorophores whose quantum yields increase substantially if noncovalently or covalently bound to proteins. Due to their strong absorptions between 550 and 700 nm they are excitable by light-emitting diodes or diode lasers. Their high absorbances (epsilon around 100,000) and adequate fluorescence quantum yields (phi up to 0.68 if bound to proteins) along with their availability as reactive NHS esters make them viable labels for proteins and oligomers, e.g. in context with SMD or fluorescence energy transfer immunoassay which is demonstrated for the system HSA/anti-HSA.

Fluorescent Dyes↗

PubMed1996

[Psychophysiologic and psychologic correlates of the emotional family climate in schizophrenic patients and their family].

Within the framework of the vulnerability-stress model of schizophrenia, it is assumed that there is a specific relationship between the factors "expressed emotion" in the family of the patients and "psychophysological activation" of the patients. High expressed emotion would go together with a rise in psychophysiological activation. The aim of this study was to test whether psychophysiological correlates of an emotional family atmosphere could be found in the case of 2 schizophrenic patients in remission and their relatives (parents). The patients and their respective relatives were examined psychophysiologically during a baseline condition (alone), non-verbal interaction, and a discussion of relevant conflict areas. Among other things, three electrodermal parameters were recorded as autonomous measures of activation: SCL, number and amplitudes of nsSCs. The Camberwell Family Interview was used for assignment of EE. In addition, psyhopathological symptoms, reciprocal behavior assessment and agreement in various areas of life with self-assessment scales were recorded for patients and relatives. Despite the effectiveness of the experimental conditions, the EE categories were not reflected in any of the recorded measurements on the psychophysiological level. However, the EE categories were clearly reflected in the psychological parameters. HEE relatives proved to be less in agreement with others within the family, and they tended to be psychopathologically more conspicuous. The mutual behavior assessment for HEE couples was more negative than for LEE couples. The overlapping effects that could be a possible explanation of the psychophysiological findings and the results of the psychological correlates are discussed. Possibilities for improvement and further research strategies are suggested.

Adult↗

PubMed1987

The molecular organization of the lysostaphin gene and its sequences repeated in tandem.

The gene encoding lysostaphin of Staphylococcus staphylolyticus was cloned in Escherichia coli and its DNA sequence was determined. The complete coding region comprises 1440 base pairs corresponding to a precursor of 480 amino acids (molecular weight 51 669). It was shown by NH2-terminal amino acid sequence analysis of the purified extracellular lysostaphin from S. staphylolyticus that the mature lysostaphin consists of 246 amino acid residues (molecular weight 26926). Polyacrylamide gel electrophoresis revealed a similar molecular weight for the most active form. By computer analysis the secondary protein structure was predicted. It revealed three distinct regions in the precursor protein: a typical signal peptide (ca. 38 aa), a hydrophilic and highly ordered protein domain with 14 repetitive sequences (296 aa) and the hydrophobic mature lysostaphin. The lysostaphin precursor protein appears to be organized as a preprolysostaphin.

Amino Acid Sequence↗

PubMed1973