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  • 1
    Electronic Resource
    Electronic Resource
    Colloidal carriers for intravenous drug targeting: Plasma protein adsorption patterns on surface-modified latex particles evaluated by two-dimensional polyacrylamide gel electrophoresis (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 1382-1387 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Targeting to specific sites of the body via colloidal carriers is sought in order to reduce drug side effects. The adsorption of plasma proteins on intravenously injected particles is regarded as the key factor in explaining their organ distribution: total bound protein, or, more likely, the presence of specific proteins and their conformation, are expected to influence macrophage uptake. Polystyrene beads, 60 nm in diameter, were used as model carriers; their surface was differentially modified by adsorption of increasingly hydrophilic block copolymers, poloxamers 184, 188 and 407. After incubation in plasma, the patterns of protein adsorption onto coated beads were analyzed by high-resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The behavior of some representative proteins was monitored, including albumin, fibrinogen, IgG, factor B and the apolipoproteins, A-I, A-IV, C-III, E and J. The more hydrophobic the particles, the larger the total amount of bound protein. However, this correlation was not valid for all of the analyzed protein species, which proves that it is insufficient to look only at physico-chemical data to predict organ distribution. On the contrary, it is essential to use 2-D PAGE to establish the correlation between adsorbed proteins and carrier behavior in vivo.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401214
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  • 2
    Electronic Resource
    Electronic Resource
    High-performance human myocardial two-dimensional electrophoresis database: Edition 1996 (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 1700-1712 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Protein sequencing ; Amino acid analysis ; Matrix assisted laser desorption ionization-mass spectrometry ; Database ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The master gel of the human myocardial two-dimensional electrophoresis (2-DE) gel database contains about 3300 protein spots characterized in terms of isoelectric point (pI) and molecular mass. A high-performance technique was applied, using large gels (23 × 30 cm). Isoelectric focusing with anodic sample preparation and nonequilibrium running conditions (NEPHGE) was combined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in 15% acrylamide gels in the second dimension. The range of pI extends from pH 4.5 to 9.6. Seventy proteins were identified by combinations of amino acid analysis, N-terminal and internal sequencing, immunostaining, matrix assisted laser desorption/ionization-mass spectrometry (MALDI-MS) peptide mass fingerprinting, post-source decay MALDI-MS and ladder sequencing by carboxypeptidase P. The identification of additional proteins, not found in the master gel, was achieved by immunoblotting. Unequivocal identification with high sensitivity and good yield was obtained by combining internal sequencing and MALDI-MS. In-gel digestion, the concentration and purification of peptides in a peptide collecting device, and the improved FRAGMOD program for peptide mass fingerprinting have added to the security and sensitivity of identification. The high-performance human myocardial 2-DE database was built up with proteins detected by the TOPSPOT program. Spots within six sections of the whole pattern are clickable. Protein description includes detailed information about identification, characterization, and links to the related SWISS-PROT, other 2-DE databases and Medline entries. The database is constructed in accordance with four of the rules for a federated database.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150171107
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  • 3
    Electronic Resource
    Electronic Resource
    Die Kristallstruktur von KPdMIVF7 (MIV = Zr, Hf) (1995)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 621 (1995), S. 1047-1052 
    Details
    ISSN: 0044-2313
    Keywords: Zirconium fluoride ; hafnium fluoride ; ternary fluorides ; KPdMIVF7 (MIV = Zr, Hf) ; crystal structure ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: The Crystal Structure of KPdMIVF7 (MIV = Zr, Hf)Blue single crystals of KPdZrF7 are obtained by heating the binary fluorides in sealed Pt-tubes under dry argon (solid state reaction, T ≍ 720°C, t ≍ 14 d). The compound crystallizes orthorhombically in the space group Pnna-D2h6 (Nr. 52); lattice parameters are a = 1 132.3(5) pm, b = 797.5(2) pm, c = 639.8(1) pm; Z = 4 (Four cycle diffractometer data, AED2). According to [F4PdF2/1ZrF5] distortet [PdF6]-octaedra are connected with pentagonal-bipyramidal [ZrF7]-polyhedra via two bridging F-, resulting in [PdZrF11]-groups. These [PdZrF11]-groups built up a threedimensional-network with K+ in its spacings. KPdHfF7 crystallizes isotypically (a = 1 136.1(3) pm, b = 796.4(2) pm und c = 638.8(1) pm; four cycle diffractometer data, AED2).
    Notes: Durch Tempern der binären Fluoride im verschweißten Pt-Rohr unter Schutzgas (Ar, Festkörperreaktion, T ≍ 720°C, t ≍ 14d) erhält man blaue Einkristalle von KPdZrF7 [eigener Strukturtyp, orthorhombisch, Pnna-D2h6 (Nr. 52); a = 1 132,3(5) pm, b = 797,5(2) pm, c = 639,8(1) pm; Z = 4; Vierkreisdiffraktometerdaten AED2]. Pd2+ ist verzerrt oktaedrisch von 6 F- umgeben, wohingegen Zr4+ pentagonalbipyramidal von 7 F- koordiniert wird. Beide Koordinationspolyeder sind gemäß [F4PdF2/1ZrF5] kantenverknüpft und bilden mit weiteren solcher [PdZrF11]-Einheiten durch Eckenverknüpfung ein dreidimensionales Raumnetz, in dessen Lücken K+ eingelagert ist. Nach Vierkreisdiffraktometerdaten (AED2) kristallisiert KPdHfF7 isotyp (a = 1 136,1(3) pm, b = 796,4(2) pm und c = 638,8(1) pm).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19956210626
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  • 4
    Electronic Resource
    Electronic Resource
    Zur Kristallstruktur von LiPdGaF6, RbPdAlF6 und K1,06Pd0,95Fe1,05F6 (1995)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 621 (1995), S. 1385-1394 
    Details
    ISSN: 0044-2313
    Keywords: Palladium ; quaternary fluorides ; LiPdGaF6 ; RbPdAlF6 ; K1.06Pd0.95Fe1.05F6 ; crystal structure ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: The Crystal Structure of LiPdGaF6, RbPdAlF6 and K1.06Pd0.95Fe1.05F6Single crystals of LiPdGaF6 (blue; trigonal, P31c-D3d2 (No. 163), a = 505.72(2), c = 923.7(2) pm; LiCaAlF6-Type [1]), RbPdAlF6 (violet; orthorhombic, Pnma-D2h16 (No. 62), a = 729.0(1), b = 711.1(1), c = 1006.5(2) pm; CsAgFeF6-Type [2]) and K1.06Pd0.95Fe1.05F6 (greenish-blue; tetragonal, P42/mbc-D4h13 (No. 135), a = 1 279.07(7), c = 800.2(1) pm; K1,08MnFeF6-Type [3]; four cycle diffractometer data, Siemens AED2) are obtained by heating the binary fluorides in sealed Pd-tubes under dry argon [solid state reaction, T ≈ 650, t ≈ 19 d (39 d, 24 d)].
    Notes: Durch Umsetzung von äquimolaren Gemengen der binären Fluoride im verschweißten Pd-Rohr unter Schutzgas [Ar, Festkörperreaktion, T = 650°C, t = 19 d (39 d, 24 d)] erhält man Einkristalle von LiPdGaF6 (blau, trigonal, P31c-D3d2 (No. 163), a = 505,72(2), c = 923,7(2) pm, LiCaAlF6-Typ [1]), RbPdAlF6 (violett, orthorhombisch, Pnma-D2h16 (No. 62), a = 729,0(1), b = 711,1(1), c = 1006,5(2) pm, CsAgFeF6-Typ [2]) sowie K1,06Pd0,95Fe1,05F6 (blau-grün, tetragonal, P42/mbc-D4h13 (No. 135), a = 1279,07(7), c = 800,2(1) pm; K1,08MnFeF6-Typ [3]; jeweils Vierkreisdiffraktometerdaten).
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19956210818
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  • 5
    Electronic Resource
    Electronic Resource
    Cs2Cu3MIVF12 (MIV = Zr, Hf) - Kristallstruktur und magnetische Eigenschaften (1995)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 621 (1995), S. 993-1000 
    Details
    ISSN: 0044-2313
    Keywords: Zirconium(IV) fluoride ; hafnium(IV) fluoride ; Cs2Cu3MIVF12 (MIV = Zr, Hf) ; crystal structure ; magnetic properties ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Cs2Cu3MIVF12 (MIV = Zr, Hf) - Crystal Structure and Magnetic BehaviourColourless single crystals of Cs2Cu3ZrF12 are obtained by heating the binary fluorides in sealed Pt-tubes under dry argon (solid state reaction, T ≍ 700°C, t ≍ 7-10 d). The compound crystallizes trigonal-rhomboedrical in the space group R3m-D3d5 (Nr. 166); lattice parameters are a = 716.61(6) pm, c = 2 046.4(2) pm, Z = 3 (Four cycle diffractometer data, AED 2). The structure is dominated by layers of corner-sharing, Jahn-Teller-distorted [CuF6]-Octahedra, which are connected via regular [ZrF6]-Octahedra to stackings parallel [00.1]. Cs+-ions are located in the spacings of the octahedra-network. From powder data Cs2Cu3HfF12 with a = 716.32(4) pm, c = 2 048.6(2) pm is isotypic. Both compounds show antiferromagnetic behaviour already at temperatures about 200 K.
    Notes: Durch Umsetzung der binären Fluoride im verschweißten Pt-Rohr unter Schutzgas (Ar, Festkörperreaktion, T ≍ 700°C, t ≍ 20d) erhält man farblose Einkristalle von Cs2Cu3ZrF12. [Trigonal-rhomboedrisch, R3m-D3d5 (Nr. 166), a = 716,61(6) pm, c = 2 046,4(2) pm, Z = 3 (Vierkreisdiffraktometerdaten, AED 2)]. Strukturbestimmend sind Schichten eckenverknüpfter, Jahn-Teller-verzerrter [CuF6]-Oktaeder, welche - über reguläre [ZrF6]-Oktaeder verknüpft - Stapel entlang [00.1] bilden. In den Hohlräumen der Struktur sind Cs+-Ionen eingelagert. Nach Pulverdaten kristallisiert Cs2Cu3HfF12 mit a = 716,32(4) pm, c = 2 048,6(2) pm isotyp. Beide Stoffe zeigen bereits bei Temperaturen um 200 K antiferromagnetisches Verhalten.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19956210617
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  • 6
    Electronic Resource
    Electronic Resource
    Identification and characterization of heat shock protein 27 protein species in human myocardial two-dimensional electrophoresis patterns (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2823-2831 
    Details
    ISSN: 0173-0835
    Keywords: Matrix assisted laser desorption ; ionization-mass spectrometry ; Peptide mass fingerprinting ; Two-dimensional polyacrylamide gel electrophoresis ; Enzymatic in-gel digestion ; Myocardial proteins ; Heat shock protein 27 ; Phosphorylated proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Immunostaining of heat shock protein 27 (Hsp27) protein species on two-dimensional electrophoresis (2-DE) gels with enhanced sensitivity yields 59 spots reacting with anti-Hsp27 antibodies. Recombinant Hsp27 exists in 2-DE as two major protein species which comigrate in the human myocardial pattern with Hsp27 spots C754 and D899 as defined in the heart high-performance 2-DE database (http://www.mdc-berlin.de/∼emu/heart/). Preparative electrophoresis of human myocardial proteins and analysis of the enriched mass range 20-30 kDa by 2-DE revealed eight protein spots (C438, C582, C658, C697, C754, C595, C750) from the human myocardial database and a new spot not previously detected on silver-stained gels. These spots were identified as Hsp27 protein species by enzymatic in-gel-digestion and analysis by matrix assisted laser desorption-ionization (MALDI) peptide mass fingerprinting and, in part, MALDI-post source decay sequencing of single fragments. Possible post-translational modifications were investigated: immunostaining tests with anti-phospho-serine/-threonine/-tyrosine antibodies, although positive for other myocardial proteins, were negative for presumed Hsp27 protein species; likewise, periodate-glycostaining assays and biotinylation screening did not detect modifications in the investigated Hsp27 protein species.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181518
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  • 7
    Electronic Resource
    Electronic Resource
    Host: Guest chemistry of diaza-18-crown-6: Selective precipitation from mixtures of oligohydroxy phenols and the structures of five host: Guest complexes (1988)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 6 (1988), S. 491-505 
    Details
    ISSN: 1573-1111
    Keywords: Phenol ; diol ; diaza-18-crown-6 ; crystal structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Diaza-18-crown-6 (1,4,10,13-tetraoxa-7,16-diaza-cyclo-octadecane) selectively precipitates as a 1,4-dihydroxybenzene-complex from a mixture of isomeric phenols and as a 2,6-dihydroxynapthalene-complex from mixtures of isomeric diols. These selective precipitations are discussed in terms of structure and solubility of the host-guest complexes and phenol acidity. The crystal structures of diaza-18-crown-6 with guestsp-nitrophenol (2: 1), 2,4-dinitroaniline (2: 1), 5,5-diethylbarbituric acid (2: 1), salicylaldoxime (2: 1) and 1,4-dihydroxybut-2-yne (1: 1) are reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00660747
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilized xanthine oxidase: Kinetics, (in)stability, and stabilization by coimmobilization with superoxide dismutase and catalase (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1507-1522 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Milk xanthine oxidase was immobilized by covalent attachment to CNBr-activated Sepharose 4B and by adsorption to n-octylamine-substituted Sepharose 4B. The amounts of activity immobilized for the two preparations were 30 and 90%, respectively. The pH optima for free and adsorbed xanthine oxidase were at 8.6 and 8.2, respectively. Both free and immobilized xanthine oxidase show substrate inhibition. The apparent inhibition constant (Ki′) found for adsorbed xanthine oxidase with xanthine as substrate was higher than the Ki for the free enzyme, which was shown to be due to substrate diffusion limitation in the pores of the carrier beads (internal diffusion limitation). Higher substrate concentrations, as desirable for practical application in organic synthesis, can therefore be used with the immobilized enzyme without decreasing the rate. As a result of the internal diffusion limitation the apparent Michaelis constant (Km′) for adsorbed xanthine oxidase was also higher than the Km for the free enzyme. Immobilized xanthine oxidase was more stable than the free enzyme during storage at 4 and 30°C. Both forms rapidly lost activity during catalysis. The loss was proportional to the amount of substrate converted. Coimmobilization of xanthine oxidase with superoxide dismutase and catalase improved the operational stability, suggesting that O2- and H2O2 side-products of the enzymatic reaction were involved in the inactivation. Coimmobilization with albumin also had some stabilizing effect. Complete surrounding of xanthine oxidase by protein, however, by means of etrapment in a glutaraldehyde-crosslinked gelatin matrix, considerably enhanced the operational half-life. This system was less efficient than the Sepharose preparations either because much activity was lost during the immobilization procedure and/or because it had poor flow properties. Xanthine (15 mg)was converted by an adsorbed xanthine oxidase preparation and product (uric acid) was isolated in high yield (84%).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260201002
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  • 9
    Electronic Resource
    Electronic Resource
    Kinetics and stability of immobilized chicken liver xanthine dehydrogenase (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1767-1786 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Xanthine dehydrogenase (EC 1.2, 1.37) was isolated from chicken livers and immobilized by adsorption to a Sepharose derivative, prepared by reaction of n-octy-lamine with CNBr-activated Sepharose 4B. Using a crude preparation of enzyme for immobilization it was observed that relatively more activity was adsorbed that protein, but the yield of immobilized activity increased as a purer enzyme preparation was used. As more activity and protein were bound, relatively less immobilized activity was recovered. This effect was probably due to blocking of active xanthine dehydrogenase by protein impurities. The kinetics of free and immobilized xanthine dehydrogenase were studied in the pH range 7.5-9.1. The Km and V values estimated for free xanthine dehydrogenase increase as the pH increases; the K'm and V values for the immobilized enzyme go through a minimum at pH 8.1. By varying the amount of enzyme activity bound per unit volume of gel, it was shown that K'm is larger than Km as result of substrate diffusion limitation in the pores of the support material. Both free and immobilized xanthine dehydrogenase showed substrate activation at low concentrations (up to 2μM xanthine). Immobilized xanthine dehydrogenase was more stable than the free enzyme during storage in the temperature range of 4-50°C. The operational stability of immobilized xanthine dehydrogenase at 30°C was two orders of magnitude smaller than the storage stability. t½ was 9 and 800 hr, respectively. The operational stability was, however, better than that of immobilized milk xanthine oxidase (t½ = 1 hr). In addition, the amount of product formed per unit initial activity in one half-life, was higher for immobilized xanthine dehydrogenase than for immobilized xanthine oxidase. Unless immobilized milk xanthine oxidase can be considerable stabilized, immobilized chicken liver xanthine dehydrogenase is more promising for application in organic synthesis.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260211006
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  • 10
    Electronic Resource
    Electronic Resource
    Characterization of initial events in bacterial surface colonization by two Pseudomonas species using image analysis (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 1161-1170 
    Details
    ISSN: 0006-3592
    Keywords: bacterial colonization ; kinetic rates ; solidwater interfaces ; Pseudomonas aeruginosa ; Pseudomonas fluorescens ; image analysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The processes leading to bacterial colonization on solidwater interfaces are adsorption, desorption, growth, and erosion. These processes have been measured individually in situ in a flowing system in real time using image analysis. Four different substrata (copper, silicon, 316 stainless-steel and glass) and 2 different bacterial species (Pseudomonas aeruginosa and Pseudomonas fluorescens) were used in the experiments. The flow was laminar (Re = 1.4) and the shear stress was kept constant during all experiments at 0.75 N m-2. The surface roughness varied among the substrata from 0.002 μm (for silicon) to 0.015 μm (for copper). Surface free energies varied from 25.1 dynes cm-1 for silicon to 31.2 dynes cm-1 for copper. Cell curface hydrophobicity, reported as hydrocarbon partitioning values, ranged from 0.67 for Ps. fluorescens to 0.97 for Ps. aeruginosa.The adsorption rate coefficient varried by as much as a factor of 10 among the combinations of bacterial strain and substratum material, and was positively correlated with surface free energy, the surface roughness of the substratum, and the hydrophobicity of the cells. The probability of desorption decreased with increasing surface free energy and surface roughness of the substratum. Cell growth was inhibited on copper, but replication of cells overlying an initial cell layer was observed with increased exposure time to the cell-containing bulk water. A mathematical model describing cell accumulation on a substratum is presented.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260391113
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