PubMed Health⌕ Search

Biomedical subjects

H Andres

Publications and source records attributed to H Andres.

At least 19 recordsLinked to original sources
PubMed2001

Magnetic polyoxometalates: anisotropic antiferro- and ferromagnetic exchange interactions in the pentameric cobalt(II) cluster.

The ground-state properties of the pentameric Co(II) cluster [Co(3)W(D(2)O)(2)(CoW(9)O(34))(2)](12-) were investigated by combining magnetic susceptibility and low-temperature magnetization measurements with a detailed inelastic neutron scattering (INS) study on a fully deuterated polycrystalline sample of Na(12)[Co(3)W(D(2)O)(2)(CoW(9)O(34))(2)].46D(2)O. The encapsulated magnetic Co(5) unit consists of three octahedral and two tetrahedral oxo-coordinated Co(II) ions. Thus, two different types of exchange interactions are present within this cluster: a ferromagnetic interaction between the octahedral Co(II) ions and an antiferromagnetic interaction between the octahedral and the tetrahedral Co(II) ions. As a result of the single-ion anisotropy of the octahedral Co(II) ions, the appropriate exchange Hamiltonian to describe the ground-state properties of the Co(5) spin cluster is anisotropic and is expressed as H = -2 summation operator(i= x,y,z)J(1)(i)[S(1)(i)S(2)(i) + S(2)(i)S(3)(i)] + J(2)(i)[S(1)(i)S(5)(i) + S(2)(i)S(5)(i) + S(2)(i)S(6)(i) + S(3)(i)S(6)(i)], where J(1)(i) are the components of the exchange interaction between the octahedral Co(II) ions and J(2)(i) are the components of the exchange interaction between the octahedral and tetrahedral Co(II) ions (see Figure 1d). The study of the exchange interactions in the two structurally related polyoxoanions [Co(4)(H(2)O)(2)(PW(9)O(34))(2)](10)(-) and [Co(3)W(H(2)O)(2)(ZnW(9)O(34))(2)](12)(-) allowed an independent determination of the ferromagnetic exchange parameters J(1)(x) = 0.70 meV, J(1)(y) = 0.43 meV, and J(1)(z) = 1.51 meV (set a) and J(1)(x) = 1.16 meV, J(1)(y) = 1.16 meV and J(1)(z) = 1.73 meV (set b), respectively. Our analysis proved to be much more sensitive to the size and anisotropy of the antiferromagnetic exchange interaction J(2). We demonstrate that this exchange interaction exhibits a rhombic anisotropy with exchange parameters J(2)(x) = -1.24 meV, J(2)(y) = -0.53 meV, and J(2)(z) = -1.44 meV (set a) or J(1)(x) = -1.19 meV, J(1)(y) = -0.53 meV, and J(1)(z) = -1.44 meV (set b). The two parameter sets reproduce in a satisfactory manner the susceptibility, magnetization, and INS properties of the title compound.

Journal Article↗
PubMed2000

High-Spin Molecules: A Novel Cyano-Bridged MnMo Molecular Cluster with a S=51/2 Ground State and Ferromagnetic Intercluster Ordering at Low Temperatures Financial support by the Swiss National Science Foundation through Project No. 21-52699.97 and the TMR Research Network ERBFMRXCT 980181 of the European Union, entitled: "Molecular Magnetism: From Materials towards Devices" is gratefully acknowledged. The authors also thank Thierry Strässle from the Paul Scherrer Institute, Villigen, for assistance with the heat capacity measurement and Professor Fernando Palacio, University of Zaragoza, for stimulating discussions.

Explore the source record for details and available documents.

Journal Article↗
PubMed1998

Recombinant fusion proteins for the industrial production of disulfide bridge containing peptides: purification, oxidation without concatamer formation, and selective cleavage.

We report the biotechnical production of peptides of approximately 35-50 amino acids in length containing one intramolecular disulfide bridge, using a recombinant fusion tail approach. This method fills the technological gap when either (a) chemical synthesis fails due to known problematic peptide sequences or (b) if simple recombinant expression is unsuccessful due to degradation. The fusion tail described here serves several purposes: (i) it enables high expression levels in Escherichia coli to be achieved; (ii) it renders the fusion protein fairly soluble; (iii) it contains a histidine affinity tag for easy purification on Ni-chelate resins, which also serves as a catalyst for the oxygen-dependent formation of the disulfide bridge; and (iv) it suppresses the formation of concatamers during the oxidation process through steric hindrance. The purified fusion protein is then immobilized on a reversed phase column for two purposes: (i) chemical cleavage of the fusion tail by cyanogen bromide and (ii) subsequent purification of the peptide. A very hydrophilic fusion partner is required so that immobilization on the reversed phase column always occurs due to the peptide. Sensitive hydrophobic residues are thereby protected from the cleavage reagent while the cleaved hydrophilic fusion tail is easily separated from the hydrophobic peptide. The method is exemplified by eight peptides representing an immunodominant epitope of the human immunodeficiency virus, but may be useful for a significant variety of similar peptides.

Amino Acid Sequence↗
PubMed1996

[Determination of cardiac troponin I on Stratus analyzer: prospective evaluation in unstable angina].

Cardiac troponin I (troponin lc) has been measured on the Dade Stratus analyzer. Cardiac specificity has been studied in patients presenting a rhabdomyolysis syndrome. The obtained results clearly demonstrated that this parameter may be used as a specific marker of myocardial injury, in contrast to total creatine kinase- or mass CK-MB measurements. In unstable angina, two groups of patients may be defined: one group with elevated troponin lc (> 0.60 microgram/L; 31 patients, group I), one other with normal troponin lc (< 0.35 microgram/L; 49 patients; group II). Quantitative angiographic analysis was performed on 50 patients including 18 patients from group I. Group I showed a more severe culprit lesion than group II. All the results suggested that troponin Ic might be an indicator of severity in unstable angina.

Adult↗
PubMed1993

Synthesis of and radioligand binding studies with a tritiated pinacidil analogue: receptor interactions of structurally different classes of potassium channel openers and blockers.

The synthesis of N-cyano-N'-[1,1-dimethyl-[2,2,3,3-3H]propyl]-N"-(3- pyridinyl)guanidine, [3H]-15, is described. The utility of this tritiated radioligand in characterizing the interactions of potassium channel openers and blockers with their receptors is demonstrated. Potassium channel openers of the pinacidil, cromakalim, aprikalim, diazoxide, and minoxidil types, as well as KATP channel blockers of the glibenclamide and eosine types, are all capable of displacing [3H]-15 from its receptor. The results indicate that all of these compounds interact with the same target protein, but that several different allosterically coupled receptor binding sites are probably involved. The highly significant correlation between the ability of the structurally diverse potassium channel openers to inhibit [3H]-15 binding and to relax vascular smooth muscle is consistent with their receptor binding sites being closely associated with the potassium channel protein which is the functional target of this class of drugs.

Animals↗
PubMed1993

Binding of the K+ channel opener [3H]P1075 in rat isolated aorta: relationship to functional effects of openers and blockers.

P1075 [N-cyano-N'-(1,1-dimethylpropyl)-N"-3-pyridylguanidine], an analogue of the K+ channel opener pinacidil, was shown to be a K+ channel opener in rat aorta, based on (i) its ability to stimulate 86Rb+ efflux, (ii) its ability to relax contractions in response to noradrenaline under normal conditions (5 mM KCl) but not under depolarized conditions (55 mM KCl), and (iii) the sensitivity of these effects to inhibition by the sulfonylurea glibenclamide. In these assays, P1075 was approximately 20 times more potent than cromakalim. Using a tritiated derivative, [3H] P1075, specific binding could not be detected in microsomal preparations from various tissues. However, in rat aortic strips specific binding of [3H]P1075 has been observed and was reduced by lowering the temperature or by decreasing intracellular ATP levels via metabolic inhibition. Specific [3H]P1075 binding was influenced neither by depolarization (55 mM KCl) nor by lowering the pH from 7.4 to 6.0. Binding was inhibited by representatives from all major families of K+ channel openers, with potencies that correlated well with the potencies obtained in 86Rb+ efflux and relaxation studies. However, stimulation of 86Rb+ efflux occurred at 40 times higher concentrations than did binding (and vasorelaxation). Of the various inhibitors of the K+ channel openers tested, only the sulfonylureas inhibited [3H] P1075 binding with the same rank order of potencies as that required for inhibition of P1075-induced 86Rb+ efflux, although at higher concentrations. The results show that binding of [3H] P1075 is independent of membrane potential but decreases concomitantly with the intracellular ATP level. The excellent correlation between the potencies of the openers and sulfonylurea blockers in binding assays and functional studies suggests that the 'drug receptor' labeled by [3H]P1075 in rat isolated aorta is of functional relevance. However, the fact that binding of the openers occurred at concentrations considerably lower than those required for K+ channel opening and that binding of the sulfonylureas was only reflected at concentrations higher than those needed to block the channel requires complex models to link binding and effect, possibly involving two agonist binding sites coupled by negative cooperativity.

Adenosine Triphosphate↗
PubMed1992

Identification of a specific binding site for K+ channel openers in rat aorta.

The K+ channel openers (KCOs) form a structurally heterogeneous group of compounds which relax smooth muscle by opening K+ channels in the plasmalemma. At present it is not known whether these drugs open the same K+ channel in smooth muscle and, if so, whether they bind to the same site of this channel. To address these questions we present the first binding study with KCOs in a smooth muscle preparation. In intact rat aortic strips, the novel tritiated KCO, 3H-P1075 (N-cyano-N'-(1,1-dimethyl[2,2,3,3(3)H]propyl)-N"-3-pyridylguanidine++ +), a potent pinacidil analogue, showed saturable specific binding of high affinity (KD = 6 +/- 1 nM, Bmax = 23 +/- 3 fmol/mg tissue wet weight). Specific binding of 3H-P1075 was inhibited stereospecifically by representatives from all major families of K+ channel openers, with a rank order of potency that correlated well with the potencies for vasorelaxation in rat aorta. The sulfonylurea glibenclamide, a relatively specific blocker of ATP-sensitive K+ channels and an inhibitor of the effects of KCOs, also inhibited 3H-P1075 binding and increased the rate of dissociation of 3H-P1075 from the tissue in a concentration-dependent manner. Lowering temperature (from 37 degrees C to 2 degrees C) and decreasing intracellular ATP levels by metabolic poisoning, diminished specific 3H-P1075 binding by reducing Bmax. However, depolarization (KCl = 55 mM) or lowering pH from 7.4 to 6.0 did not influence binding. The data demonstrate the existence of a specific binding site for the KCO 3H-P10756 in rat isolated aorta, which seems to be of functional relevance.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1988

The order and orientation of mouse lambda-genes explain lambda-rearrangement patterns.

Mouse lambda-genes are rearranged in specific V lambda-JC lambda associations: V lambda 1 has only been found to rearrange with JC lambda 3 or JC lambda 1, whereas V lambda 2 mainly rearranges with JC lambda 2 and very rarely with JC lambda 1,3. In order to determine the physical basis for these associations we have cloned the respective lambda-genes and large portions of their flanking regions by chromosomal walking in a total of 141 kb of phage and cosmid clones. With the use of unique probes obtained from such clones, the order and orientation of the mouse lambda-gene segments were determined by analyzing patterns of DNA deletion associated with lambda-gene rearrangements in various cell lines. All V and C gene segments were found to be in the same transcriptional orientation, and V2 and V1 were found not to be next to each other, thus supporting the gene order V2-C2-C4-V1-C3-C1.

Animals↗
PubMed1986

Fatty-acid biosynthesis in man, a pathway of minor importance. Purification, optimal assay conditions, and organ distribution of fatty-acid synthase.

Fatty-acid synthase has been purified to homogeneity from human liver by a 3-step procedure including protamine sulfate/ammonium sulfate fractionation, affinity chromatography on 2',5'-ADP-Sepharose 4B and gel filtration on Sephacryl S-300. Both the human and rat fatty-acid synthase had similar characteristics regarding molecular mass, subunit structure, amino-acid composition, and substrate affinities. In order to measure the fatty-acid synthase activities in small tissue samples it was necessary to improve the sensitivity of an isotopic assay using [14C]malonyl-CoA as tracer. Special attention was paid to the dual role of free CoASH as an activator and inhibitor of the enzyme. Considerable differences existed between the specific activities of the fatty-acid synthase complex measured in human and rat lipogenic organs. Only negligible values of about 1 mU/mg protein were found in human liver and adipose tissue, while the corresponding activities were 10- to 50-fold higher in young lean rats. Less pronounced but still remarkable differences were determined for the activity of the acetyltransferase which catalyses the initial primer reaction of the fatty-acid synthase complex. In some selected cases under long-term fat-free diet (alcoholism, parenteral nutrition) elevated values of fatty-acid synthase activities were detected in human tissues. Under usual diet, with a relatively high fat content of up to 40 percent, and even after a carbohydrate-rich diet for three days, fatty-acid synthase activity remained low. It is concluded that under the dietary conditions, common for the industrialized world, de novo lipogenesis in man is negligible.

Adipose Tissue↗
PubMed1985

Submucosal plexus and electrolyte transport across rat colonic mucosa.

Electrolyte transport across two preparations of mucosa from rat colon descendens was compared to determine what influence the submucosal plexus has on electrolyte transport. One preparation consisted of the mucosa, muscularis mucosae, and the submucosal tissue and is referred to as the mucosa-submucosa preparation. The second preparation obtained by further blunt dissection of the mucosa-submucosa preparation consisted of only the mucosa and the circular muscle layer of muscularis mucosae and is referred to as the mucosa preparation. Histological studies showed that the submucosal tissue and the longitudinal layer of muscularis mucosae could be removed leaving only the mucosa and the circular layer of muscularis mucosae. The extensive neuronal network of the submucosa was shown when the submucosal tissue and longitudinal muscle layer of muscularis mucosae, which were removed, were stained histochemically for acetylcholinesterase activity. Both the mucosa-submucosa and mucosa preparations absorbed Na+ and Cl- when short-circuited. However, Na+ and Cl- absorption were significantly higher in the mucosa preparation. The increase in Na+ and Cl- transport in the mucosa preparation was accompanied with a decrease in the short-circuit current (Isc), the open-circuit potential difference (p.d.) and the transmural tissue conductance (Gt) when compared to the mucosa-submucosa preparation. Tetrodotoxin (TTX), a neurotoxin which blocks specifically the propagation of action potentials in excitable tissues, dose-dependently decreased Isc and p.d. in the mucosa-submucosa preparation when added to the serosal solution. The half-maximal effective concentration of TTX was 5 nM and maximal effective concentration 100 nM. TTX (1 microM) had no effect on Isc or p.d. when added to the mucosal solution. The decrease in Isc and p.d. caused by TTX in the mucosa-submucosa preparation was accompanied with an increase in Na+ and Cl- absorption. TTX caused only a small decrease in Isc and p.d. in the mucosa preparation. However, there was no measurable change in Na+ and Cl- transport in the mucosa preparation. The results suggest that spontaneously active neurones from the submucosal plexus have an inhibitory influence on the mucosa. Physical removal of the submucosal plexus or pharmacological blockade of the neurones within the mucosa-submucosa preparation by TTX led to enhanced absorption, suggesting that the set point of the mucosa for electrolyte transport is at or near a maximal absorptive state. Regulation or modulation of the mucosa may therefore occur by mechanisms that lower this set point, causing an inhibition of absorption of electrolytes.

Animals↗
PubMed1984

Immunoassay of ergotamine and dihydroergotamine using a common 3H-labelled ligand as tracer for specific antibody and means to overcome experienced pitfalls.

A highly sensitive radioimmunoassay for the determination of ergotamine and dihydroergotamine is described. The limit of detection is about 9 pg/mL blood plasma for both compounds. The specificity of the gamma-globulin, which was prepared from rabbit antiserum, was investigated in the presence of compounds synthesized as possible metabolites. It was found that the tricyclic peptide moiety common to both molecules is an essential structural feature for binding to the gamma-globulin. From dilution experiments with the radioactively labelled compound it followed that ergotamine and to a lesser extent also its dihydro derivative are adsorbed on various tube wall materials using known buffer solutions. A practically insuperable obstacle is rearrangement of ergotamine under the experimental conditions, forming a stereoisomer by inversion at the C-8 position. The equilibrium of ergotamine in equilibrium ergotaminine found in human plasma remains stable under the incubation conditions of the radioimmunoassay.

Dihydroergotamine↗
PubMed1980

Properties and organ distribution of ATP citrate (pro-3S)-lyase.

1. The lipogenic enzyme ATP citrate lyase (ATP:citrate oxaloacetate-lyase (pro-3S-CH2COO-acetyl-CoA; ATP-dephosphorylating), EC 4.1.3.8) is partially purified from human liver by ammonium sulfate fractionation and anionexchange chromatography. 2. Km values for the substrates are 1.1 x 10(-5) 1.3 x 10(-3), and 1.2 x 10(-4) M for CoASH, ATP and citrate, respectively. The hypolipidemic drug L(-)-hydroxycitrate is a competitive inhibitor with respect to citrate (Ki = 3 x 10(-4) M). 3. Specific activities measured in liver, adipose tissue and intestinal mucosa (autopsic and biopsic material) are in the range of 1 mU/mg protein suggesting that the citrate pathway does not significantly contribute to human lipogenesis. No stimulation is found after a 3-day carbohydrate-rich diet. 4. Specific activities of other key-enzymes of the acetyl-CoA production from carbohydrates (pyruvate dehydrogenase, cytosolic acetyl-CoA synthetase) are of the same low magnitude.

ATP Citrate (pro-S)-Lyase↗