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Biomedical subjects

G Braun

Publications and source records attributed to G Braun.

At least 55 records · Page 3Linked to original sources
PubMed1989

Cerebral and peripheral demethylation of psychotomimetics measured by expired 14CO2.

Demethylation of psychotomimetic compounds was measured by labeling each methyl and methoxy substitutent separately with 14C and injecting it into rats, intravenously and intracerebrally. Expired [14C]CO2 was measured continuously and the resultant multi-exponential curves yielded rates and integral demethylation. 5-Methoxy-N,N-dimethyltryptamine was not demethylated, eliminating one proposed metabolic pathway. 2,4,5-Trimethoxyphenalkylamines were demethylated less in the brain than peripherally, markedly so at the p-methoxy position, suggesting a possible biochemical site for endogenous induction of psychosis.

Amphetamines↗
PubMed1988

Isolation and in vitro translation of Onchocerca volvulus mRNA.

Adult Onchocerca volvulus recovered for excised nodules by dissection or treatment with collagenase have been used as a source of RNA for in vitro translation experiments. RNA was purified using either the hot phenol/SDS procedure or the guanidine isothiocyanate protocol. Immunoprecipitation experiments performed on in vitro products demonstrate a marked heterogeneity in responses by individed human infection sera. Further immunoprecipitation experiments demonstrate cross reactivity between O. volvulus and other filarial nematodes.

Animals↗
PubMed1987

Evolution of the enterobacterial sulA gene: a component of the SOS system encoding an inhibitor of cell division.

The LexA-regulated sulA (sfiA) gene of Escherichia coli encodes an unstable protein which inhibits cell division. By determining the nucleotide sequences of the corresponding genes from the related bacteria Salmonella typhimurium, Enterobacter aerogenes and Serratia marcescens it was found that the regulatory region and the LexA binding site (SOS box) have been better conserved during evolution than the coding sequence. The N terminus of the SulA protein [amino acid (aa) residues 1-30] has diverged extensively during the evolution of Enterobacteriaceae, whereas the central region (aa residues 31-149) has been well conserved. At the C terminus a sequence showing some homology to the N protein of phage lambda was detected that may represent a recognition site for the Lon protease, which is known to degrade both polypeptides. When expressed in E. coli, the foreign sulA genes did not block cell division suggesting that their products are inactive. This may indicate that the N terminus of the SulA protein is involved in recognizing the cell division apparatus.

Amino Acid Sequence↗
PubMed1986

Critical evaluation of platelet aggregation in whole human blood.

Platelet aggregation studies generally are performed in platelet-rich plasma (PRP) by the turbidometric method. The authors compared this technic with the recently introduced impedance aggregometry in PRP and whole blood (WB). In healthy controls there was a good correlation between the two technics when aggregation was induced by ADP or collagen. As compared with PRP, platelets in WB were more sensitive to the aggregating effect of thrombin, ristocetin, and arachidonic acid. Platelet sensitivity to prostacyclin was increased in WB. The anti-platelet effect of a single oral dose of aspirin could be detected for a longer period in WB than in PRP. Platelet aggregation tests in WB from patients with platelet dysfunctions showed the same response pattern to different aggregating agents as in PRP. In contrast to turbidometry, the impedance method in PRP and WB enabled registration of platelet aggregation in a dose-dependent fashion in a sample from a patient with severe hyperlipoproteinemia. It is concluded that platelet aggregation can be studied conveniently with the impedance method in the more physiologic medium of WB. Providing the same information as the well-established turbidometry, the time-sparing impedance method needs less citrated blood. Moreover, our results show an increased sensitivity of the WB system to some aggregating and anti-platelet agents.

Adenosine Diphosphate↗
PubMed1986

Computer analysis of some bacteriological, biological and physiochemical parameters of the coastal water of Lake Balaton.

Some 61 coastal water samples were taken at four definite points of Balaton Lake. Seventeen parameters of each sample characterizing the quality of the water were studied by means of multiple correlation and regression analysis, one-way variance analysis and by factor analysis with the help of BMD computer program. Uni- and multilateral relationships could be observed among the single parameters. On the basis of the results of factor analysis six factors--phytoplankton system, anthropogenic effect, own bacterial system of the lake, nitrogen circulation, hydrocarbonate and reactive phosphate system and NH+4 circulation--could be separated. Significant qualitative differences could be found along the longitudinal axis of Balaton. It could be also demonstrated that the water of the lake in its present condition is suitable for the proliferation of bacteria. Further and deeper examinations are necessary for a better understanding of the biochemical and biological processes.

Analysis of Variance↗
PubMed1985

Effect of cholesterol on Ca2+-induced aggregation and fusion of sonicated phosphatidylserine/cholesterol vesicles.

Small unilamellar vesicles composed of phosphatidylserine (PS) and cholesterol at various ratios were employed in studying the effect of cholesterol on Ca2+-induced vesicle aggregation and fusion using the Tb/dipicolinic acid assay. The leakage of preencapsulated Tb3+ was also measured. The analysis of the data provided estimates for the rate of aggregation C11, and the rate of fusion per se, f11. An increase in cholesterol contents results in a decrease in C11 values. Similarly, aggregation of PS/cholesterol vesicles is slower than that of PS vesicles in the presence of 650 mM NaCl. With 100 or 200 mM NaCl, the overall fusion rate of PS/cholesterol vesicles is slower than that of PS vesicles; the rate being reduced by an increase in cholesterol contents. With 600 mM NaCl, the overall fusion rate of PS/cholesterol 9:1 vesicles is faster than that of PS vesicles, and results are well-simulated by assuming no delay in vesicle aggregation up to dimers. Emerging f11 values are larger in PS/cholesterol than in PS vesicles. An analysis of fusion kinetics of several lipid concentrations shows that f11 values of PS/cholesterol 3:1 vesicles are 5-times larger than those of PS vesicles, when fusion occurs in a medium containing 200 mM NaCl and 1.5 mM Ca2+. The increase in Na+ concentration from 100 to 200 mM, or 600 mM results in a 50- or 150-fold reduction in f11 values of PS vesicles. It is suggested that incorporation of cholesterol in PS vesicles results in enhancement of Ca2+-induced fusogenic capacity.

Calcium↗
PubMed1985

Rapid yeast DNA staining method for flow cytometry.

The variation of the fluorescence intensity of olivomycin-stained yeast cells as a function of the concentration of olivomycin, NaCl, and MgCl2 in the staining solution was studied. The best results were obtained when the staining solution contained 100 micrograms, olivomycin/ml, 40 mM MgCl2, and 1 M NaCl. A staining time of 12 min was sufficient for proper staining.

DNA, Fungal↗
PubMed1985

Lethal mutations in the structural gene of an outer membrane protein (OmpA) of Escherichia coli K12.

The gene ompA encodes a major outer membrane protein of Escherichia coli. Localized mutagenesis of the part of the gene corresponding to the 21-residue signal sequence and the first 45 residues of the protein resulted in alterations which caused cell lysis when expressed. DNA sequence analyses revealed that in one mutant type the last CO2H-terminal residue of the signal sequence, alanine, was replaced by valine. The proteolytic removal of the signal peptide was much delayed and most of the unprocessed precursor protein was fractioned with the outer membrane. However, this precursor was completely soluble in sodium lauryl sarcosinate which does not solubilize the OmpA protein or fragments thereof present in the outer membrane. Synthesis of the mutant protein did not inhibit processing of the OmpA or OmpF proteins. In the other mutant type, multiple mutational alterations had occurred leading to four amino acid substitutions in the signal sequence and two affecting the first two residues of the mature protein. A reduced rate of processing could not be clearly demonstrated. Membrane fractionation suggested that small amounts of this precursor were associated with the plasma membrane but synthesis of this mutant protein also did not inhibit processing of the wild-type OmpA or OmpF proteins. Several lines of evidence left no doubt that the mature mutant protein is stably incorporated into the outer membrane. It is suggested that the presence, in the outer membrane, of the mutant precursor protein in the former case, or of the mutant protein in the latter case perturbs the membrane architecture enough to cause cell death.

Amino Acid Sequence↗
PubMed1985

Xanthogranulomatous pyelonephritis in children.

Xanthogranulomatous pyelonephritis usually occurs in women 50 to 60 years old, and has the distinct clinical presentation suggestive of a renal mass. Since 1963 an increasing number of children with xanthogranulomatous pyelonephritis have been reported in the literature, with data suggesting that the characteristics of the disease are different from those in adults. We compared our children with xanthogranulomatous pyelonephritis to adults who had been described in the literature and to our cases of chronic pyelonephritis to determine whether xanthogranulomatous pyelonephritis in children is an entity as clearly different from chronic pyelonephritis as it is in adults. Twenty-one cases were eliminated from the study because of incomplete charts. We found 39 cases in which nephrectomy had been done for an anatomical diagnosis of chronic or xanthogranulomatous (8) pyelonephritis. Average age at presentation, duration of clinical course and sex distribution were similar in both groups. The left kidney was involved more often in both groups. Severe malnutrition, urolithiasis, reno-cutaneous fistula and negative urine cultures were more frequent in cases of xanthogranulomatous pyelonephritis, while obstructive nonlithiasic uropathy occurred more often in cases of chronic pyelonephritis. Microorganisms were similar in both groups and Escherichia coli was isolated most frequently. All cases of xanthogranulomatous pyelonephritis were of the diffuse type with areas corresponding to all histological stages. Our study suggests that perhaps in children xanthogranulomatous pyelonephritis occurs the same as chronic pyelonephritis, and is determined possibly by an affected immune response secondary to malnutrition and by the presence of urolithiasis.

Age Factors↗
PubMed1985

"Natural antibodies" against yeast--a flow-microfluorometric approach.

Fluorescent labeling of antibodies in connection with flow-microfluorometry was applied to "natural antibodies" against yeast strains Candida maltosa and Yarrowia lipolytica, obtained by cell column chromatography. It is shown that "natural antibodies" against these yeast strains react in a specific manner with the surface of the cells.

Animals↗
PubMed1984

DNA sequence analysis of the Serratia marcescens ompA gene: implications for the organisation of an enterobacterial outer membrane protein.

The cloned ompA gene from Serratia marcescens was fully expressed in Escherichia coli and its product correctly assembled into the outer membrane. The S. marcescens polypeptide was not functionally equivalent to the E. coli OmpA protein, which serves as a phage receptor and as a component of several colicin uptake systems. DNA sequence analysis of the gene showed that three regions of the protein likely to be exposed on the cell surface not only differed extensively from the corresponding regions of the E. coli polypeptide but also from all other sequenced OmpA proteins. It is suggested that this sequence polymorphism represents a safety mechanism by which the various enterobacterial species can avoid cross-infection by noxious agents such as phages or colicins.

Bacterial Outer Membrane Proteins↗
PubMed1983

Molecular characterization of the gene coding for major outer membrane protein OmpA from Enterobacter aerogenes.

The ompA gene from Enterobacter aerogenes was subcloned into a low-copy-number plasmid vector and the resultant plasmid, pTU7En, used to study its expression in Escherichia coli K12. Although the gene was strongly expressed and large amounts of OmpA protein were present in the outer membrane its product was not functionally identical to the E. coli polypeptide. In particular, the E. aerogenes OmpA protein was unable to confer sensitivity to OmpA-specific phages of E. coli. When the primary structure of the protein was deduced from the nucleotide sequence of its gene it was found that three domains differed extensively from the corresponding regions of the E. coli protein. As two of these are known to be exposed on the cell surface we inferred that these alterations are responsible for differences in the biological activity of the two proteins.

Bacterial Outer Membrane Proteins↗
PubMed1982

The nucleotide sequence coding for major outer membrane protein OmpA of Shigella dysenteriae.

The nucleotide sequence of the ompA gene from Shigella dysenteriae has been determined and the amino acid sequence of the pro-OmpA protein predicted. Sequence comparison between the ompA genes of S.dysenteriae and Escherichia coli showed that features such as mRNA secondary structure and codon usage, as well as polypeptide function, have been conserved during evolution. The pro-OmpA protein of S.dysenteriae consists of 351 residues, as opposed to the 346 of the E.coli protein and also shows several amino acid changes. These changes have been used to interpret differences in the biological activity of the two proteins.

Amino Acid Sequence↗