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  • Biochemistry and Biotechnology  (9)
  • Electrochemical detection  (3)
  • brain  (3)
  • 1
    Digitale Medien
    Digitale Medien
    Growth and analysis of crystal forms of toxic shock syndrome toxin 1 (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 17 (1993), S. 329-334 
    Details
    ISSN: 0887-3585
    Schlagwort(e): bacterial toxins ; superantigens ; X-ray crystallography ; crystallization ; Staphylococcus aureus ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: Native toxic shock syndrom toxin 1 (TSST-1) purified from Staphylococcus aurius has been crystallized in four different forms. The highest resolution data (2.05 Å) was collected from orthorhombic crystals belonging to the space group C2221. The unit cell dimension are a = 108.7 Å, b = 177.5 Å, c = 97.6 Å. Rotation function analysis of this from indicates that there is trimer of toxin molecules in the asymmetric unit with a local 3-fold axis parallel to the crystallographic c axis. Crystals of a double mutant of TSST-1 have been grown which has a single molecule in the asymmetric unit and diffract to 1.9 Å. The space group is P21 with unit cell parameters of a = 44.4 Å, b = 34.0 Å, c = 55.2 Å, β = 93.0°. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340170310
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  • 2
    Digitale Medien
    Digitale Medien
    Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 Å resolution: Implications for ATCase mutants and the mechanism of negative cooperativity (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 15 (1993), S. 147-176 
    Details
    ISSN: 0887-3585
    Schlagwort(e): X-ray crystallography ; pAR5 mutant ; allosteric enzyme ; ligand-induced negative cooperativity ; alternative amino acid conformations ; coordinate error ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The X-ray crystal structure of CTP-ligated T state aspartate transcarbamoylase has been refined to an R factor of 0.182 at 2.5 Å resolution using the computer program X-PLOR. The structure contains 81 sites for solvent and has rms deviations from ideality in bond lengths and bond angles of 0.018 Å and 3.722°, respectively. The cytosine base of CTP interacts with the main chain carbonyl oxygens of rTyr-89 and rIle-12, the main chain NH of rIle-12, and the amino group of rLys-60. The ribose hydroxyls form polar contacts with the amino group of rLys-60, a carboxylate oxygen of rAsp-19, and the main chain carbonyl oxygen of rVal-9. The phosphate oxygens of CTP interact with the amino group of rLys-94, the hydroxyl of rThr-82, and an imidazole nitrogen of rHis-20. Recent mutagenesis experiments evaluated in parallel with the structure reported here indicate that alterations in the hydrogen bonding environment of the side chain of rAsn-111 may be responsible for the homotropic behavior of the pAR5 mutant of ATCase. The location of the first seven residues of the regulatory chain has been identified for the first time in a refined ATCase crystal structure, and the proximity of this portion of the regulatory chain to the allosteric site suggests a potential role for these residues in nucleotide binding to the enzyme. Finally, a series of amino acid side chain rearrangements leading from the R1 CTP allosteric to the R6 CTP allosteric site has been identified which may constitute the molecular mechanism of distinct CTP binding sites on ATCase. © 1993 Wiley-Liss, Inc.
    Zusätzliches Material: 16 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340150206
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  • 3
    Digitale Medien
    Digitale Medien
    Grain sorghum stillage recycling: Effect on ethanol yield and stillage quality (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1735-1738 
    Details
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Stillage obtained from ethanol production of grain sorghum was separated into two fractions: thin stillage and wet solids. A portion of the thin stillage was recycled as cooking water in subsequent fermentation runs using both bench- and full-scale ethanol production plants. When thin stillage replaced 50-75% of the cooking water, large increases occurred in solids content, COD, and EC of the resulting thin stillage. It was found that while the volume of thin stillage requiring treatment or disposal was reduced, there was little reduction in the total pollutant load. Stillage rcycling had little effect on the quality of the stillage wet solids fraction. At the high levels of stillage recycle used, ethanol yield was reduced after three to five runs of consecutive recycling.
    Zusätzliches Material: 5 Tab.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/bit.260271217
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  • 4
    Digitale Medien
    Digitale Medien
    Effect of centrifugation on the viability of Burkitt lymphoma cellsContribution No. 1126 from the Department of Nutrition and Food Science, Massachusetts Institute of Technology. Presented at the 154th National Meeting of the American Chemical Society, Chicago, Illinois, September 10-15, 1967. (1968)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 10 (1968), S. 641-649 
    Details
    ISSN: 0006-3592
    Schlagwort(e): Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: This study reports some findings on the effects of centrifugation on the viability of mammalian cells. The authors used Burkitt lymphoma cells cultivated in a synthetic medium containing 10% fetal calf serum for all experiments. Batch centrifugations were conducted in a RC2-B centrifuge (Ivan Sorvall, Incorporated, Norwalk, Connecticut USA) operated at 0 and 25°C. During centrifugation we exposed the cells to gravitational fields ranging from 24,800 to 42.200g. The results showed that at, 0°C and 25,800 or 42,000g no loss in cell viability occurred for up to 90 min exposures in the centrifugal field. However, at 25°C and for gravitational fields of 24,800 and 42,000g, there were appreciable losses in cell viability. Continuous centrifugation studies in the Sharples supercentrifuge (Division of Penn Salt Corporation, Warminister, Pennsylvania USA) were also conducted with bowl speeds up to 28,000 rpm (19,000g) and flow rates ranging from 1.4 to 20 1, hr. Slight, losses in cell viability were noted and postulated as caused by the shear stresses encountered by the cells. Some pumping studies using the lymphoma cells substantiate this conclusion.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/bit.260100509
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  • 5
    Digitale Medien
    Digitale Medien
    Release of norepinephrine and dopamine from brain vesicular preparations: Effects of adenosine analogues (1982)
    Springer
    Cellular and molecular neurobiology 2 (1982), S. 193-204 
    Details
    ISSN: 1573-6830
    Schlagwort(e): adenosine ; catecholamines ; neurotransmission ; calcium ; brain ; striatum
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary 1. Adenosine analogues inhibit calcium-dependent K+-evoked release of [3H]norepinephrine from guinea pig cerebral cortical and hippocampal vesicular preparations. Inhibition requires high concentrations (100µM) of the adenosine analogues and is abolished in the presence of high concentrations (2 mM) of calcium ions. The inhibitory effect of 2-chloroadenosine is blocked by theophylline. The structure activity profile (N 6-d-phenylisopropyladenosine ≥N 6-l-phenylisopropyladenosine ≥ 2-chloroadenosine 〉N 6-cyclohexyladenosine, adenosine 5′-cyclopropylcar-boxamide) is not that expected of either A1 (high-affinity) or A2 (low-affinity) adenosine receptors. 2. Calcium-dependent K+-evoked release of [3H]dopamine from guinea pig striatal vesicular preparations is inhibited by apomorphine. However, only 2-chloroadenoine causes an inhibition of K+-evoked release of [3H]dopamine. Other adenosine analogues such asd- andl-phenylisopropyladenosine and adenosine 5′-cyclopropylcar-boxamide cause a facilitation of K+-evoked release. The facilitation is abolished or reduced in the presence of high concentrations (2 mM) of calcium ions. The sites of action of adenosine analogues do not appear to have structural requirements identical to those expected of A1 (high-affinity) or A2 (low-affinity) adenosine receptors. 3. The results indicate that adenosine analogues can have either inhibitory or facilitory effects on K+-evoked release of catecholamines from central synaptic terminals.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00711147
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  • 6
    Digitale Medien
    Digitale Medien
    Release of norepinephrine from brain vesicular preparations: Effects of an adenylate cyclase activator, forskolin, and a phosphodiesterase inhibitor (1982)
    Springer
    Cellular and molecular neurobiology 2 (1982), S. 179-192 
    Details
    ISSN: 1573-6830
    Schlagwort(e): adenylate cyclase ; catecholamines ; adrenergic receptors ; cyclic AMP ; phosphodiesterase ; neurotransmission ; calcium ; brain
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary 1. The calcium-dependent K+-evoked release of [3H]norepinephrine from guinea pig cerebral cortical vesicular preparations is inhibited by norepinephrine, clonidine, and epinephrine. Isoproterenol has no effect and phentolamine prevents the inhibition by norepinephrine. The results indicate that anα-adrenergic receptor mediates an inhibitory input to the calcium-dependent release process. The inhibition by norepinephrine is prevented by high concentrations (3.0 mM) of calcium ions. 2. A cyclic AMP phosphodiesterase inhibitor, ZK 62771, slightly elevates [3H]cyclic AMP levels in the guinea pig cerebral cortical preparation and potentiates the marked elevation of [3H]cyclic AMP elicited by the adenylate cyclase activator, forskolin. 3. Neither ZK 62771 nor forskolin alone has significant effects on K+-evoked release of [3H]norepinephrine from the cerebral cortical vesicular preparation; however, a combination of ZK 62771 and forskolin inhibits K+-evoked release by as much as 60%. The inhibition is reversed by high concentrations (2.0 mM) of calcium ions. The results suggest that a marked accumulation of cyclic AMP elicited via both activation of adenylate cyclase and inhibition of phosphodiesterase can be inhibitory to neurotransmitter release from central synaptic terminals.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00711146
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  • 7
    Digitale Medien
    Digitale Medien
    Release of norepinephrine and dopamine from brain vesicular preparations: Effects of calcium antagonists (1982)
    Springer
    Cellular and molecular neurobiology 2 (1982), S. 205-213 
    Details
    ISSN: 1573-6830
    Schlagwort(e): calcium ; catecholamines ; neurotransmission ; brain ; striatum ; calcium antagonists
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary 1. The calcium antagonists D-600 (1–10µM) and diltiazem (10–25µM) inhibit K+-evoked release of [3H]norepinephrine from guinea pig cerebral cortical vesicular preparations. The inhibition of release is partially reversed by increasing concentrations of calcium to 2 mM. Diltiazem at 100µM has no effect on K+-evoked release of [3H]norepinephrine at 0.15 mM calcium but does inhibit release at 2.0 mM calcium. 2. The calcium antagonist nifedipine and dantrolene, an agent purported to antagonize release of calcium from intracellular storage sites, have no effect on K+-evoked release of [3H]norepinephrine. 3. The calcium antagonists D-600 (1µM) and diltiazem (10µM) inhibit K+-evoked release of [3H]dopamine from guinea pig striatal vesicular preparations. Higher concentrations of drug, namely, 10µM for D-600 and 100µM for diltiazem, cause a potentiation rather than an inhibition of K+-evoked release. The potentiation is reduced in magnitude upon raising the extracellular calcium to 2.0 mM. Indeed, 10µM D-600 then inhibits K+-evoked release of [3H]dopamine. 4. The results indicate that putative calcium antagonists can have both inhibitory and facilitory effects on calcium-dependent K+-evoked release of catecholamines from central synaptic endings. Furthermore, certain peripheral calcium antagonists such as nifedipine and dantrolene may prove ineffective in central systems.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00711148
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  • 8
    Digitale Medien
    Digitale Medien
    A cell adhesion peptide from foot-and-mouth disease virus can direct cell targeted delivery of a functional enzyme (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 59 (1998), S. 294-301 
    Details
    ISSN: 0006-3592
    Schlagwort(e): RGD ; FMDV ; internalization ; integrins ; cell binding ; β-galactosidase ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: The G-H loop of foot-and-mouth disease virus is a disordered protrusion of the VP1 protein exposed on the virion surface. This short stretch includes an arginine-glycine-aspartic acid tripeptide, a recognized integrin-binding motif, which is responsible for cell attachment and infection. Eight copies of a peptide reproducing the amino acid sequence of this FMDV ligand have been displayed in solvent-exposed regions on an enzymatically active recombinant β-galactosidase. This viral peptide segment enables the chimeric enzyme to bind mammalian cell lines with different efficiencies, probably depending on the number of suitable cell receptors present on each of them. Moreover, it also promotes the internalization of the attached enzyme, which is transiently active inside the cells. These results suggest further exploration of the potential use of short adhesion peptides of viral origin as cell attachment tags to direct the targeted delivery of both genes and enzymes, instead of whole, infectious viruses. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:294-301, 1998.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
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  • 9
    Digitale Medien
    Digitale Medien
    Capillary electrophoresis and electrochemical detection of underivatized oligo- and polysaccharides with surfactant-controlled electroosmotic flow (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 319-324 
    Details
    ISSN: 0173-0835
    Schlagwort(e): Capillary electrophoresis ; Polysaccharides ; Electrochemical detection ; Cu electrode ; Carbohydrates ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Complex polysaccharide mixtures were analyzed directly without derivatization by capillary zone electrophoresis in strongly alkaline solutions and electrochemical detection at a Cu electrode. The positively charged surfactant cetyltrimethylammonium bromide was included in the electrophoresis medium in order to reverse the electroosmotic flow and permit elution to be in order of increasing polysaccharide size. Carbohydrate samples analyzed by this approach included linear maltoses, enzymatically hydrolyzed starch, and commercially available dextrans of up to an average molecular weight of 18 300. Detection by constant-potential oxidation at a Cu electrode was very sensitive, with detection limits for individual carbohydrates generally below the femtomole level.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/elps.1150170206
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  • 10
    Digitale Medien
    Digitale Medien
    Electrochemical detection in capillary electrophoresis with dual-parallel on-capillary electrodes (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2226-2232 
    Details
    ISSN: 0173-0835
    Schlagwort(e): Electrochemical detection ; Capillary electrophoresis ; Dual-parallel electrodes ; On-capillary electrodes ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: A new approach for dual electrode electrochemical detection in capillary electrophoresis (CEEC) is described. In this approach, two identical capillaries, each containing an on-capillary electrode incorporated permanently onto its tip, were paired together for simultaneous sample injection and detection. This procedure permitted dual-parallel detection to be performed without the need for painstaking alignment of the electrodes with respect to one another and to the capillary outlet as is required for the off-capillary microelectrode systems usually employed in CEEC. As a result, independent detection at two electrodes held at different potentials or at two electrodes of different composition or structure could be performed simply and with wide flexibility. Fabrication of on-capillary electrodes was carried out by sputter-coating the exit end of the capillaries with a thin layer of Au or Pt. Dual electrode system performance was demonstrated by separation and analysis of phenol and catechol samples. In addition, the detection system was coupled with glucose oxidase for the selective detection of glucose.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/elps.1150191230
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