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  • 1
    Electronic Resource
    Electronic Resource
    Evaluation of calcium-containing zinc electrodes in zinc/silver oxide cells (1996)
    Springer
    Journal of applied electrochemistry 26 (1996), S. 227-227 
    Details
    ISSN: 1572-8838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00364074
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  • 2
    Electronic Resource
    Electronic Resource
    Virus-like particles of calicivirus as epitope carriers (1999)
    Springer
    Archives of virology 144 (1999), S. 2429-2439 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  The VP60 of rabbit haemorrhagic disease virus (RHDV), when expressed in baculovirus, self-assembles into virus-like particles (VLP) which are antigenically and immunogenically indistinguishable from native virions. When the N-terminal 30 amino acid residues of VP60 were deleted and substituted by a well characterized six residue epitope from bluetongue virus capsid protein VP7 (Btag), the fusion protein retained its ability to self-assemble into VLPs. However, the size of these particles was only 27 nm, compared to 40 nm of VLPs derived from native VP60. The antigenicity of both VP60 and the Btag was retained as evident from ELISA and Western blot analyses. When Btag was fused at the C-terminus of VP60 without deletion, the fusion proteins formed VLPs of 40 nm in size and also retained their antigenicity, but the Btag antigenicity appeared weak at this fusion site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050655
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  • 3
    Electronic Resource
    Electronic Resource
    Topography and immunogenicity of bluetongue virus VP7 epitopes (1996)
    Springer
    Archives of virology 141 (1996), S. 111-123 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The core of bluetongue virus (BTV) consists of ten dsRNA viral genome segments and five proteins, including two major (VP7 and VP3) and three minor (VP1, VP4 and VP6) components. The major core protein VP7 is believed to be an important structural constituent because it interacts, not only with the underlying core protein VP3, but also with two outer capsid proteins (VP2 and VP5). In this communication we summarise data on the mapping of at least six different epitopes of VP7 distributed along the molecule. Two of the six epitopes have not been mapped previously. The accessibility of these epitopes in intact virions and core particles was analysed using immunoelectron microscopy. The epitope located near the N-terminus of VP7 was accessible at the surface of intact virions and core particles. Epitopes in other parts of the VP7 molecule were detected weakly in core particles but not in intact virions. These results support the proposal that VP7 molecules are orientated with their N-terminus accessible on the surface of either the particle or at least one of the three different channels observed by cryoelectron microscopy in the outer capsid layer. Analysis of the immune response to BTV-infected or -immunised sheep and rabbits to three selected epitopes, which are located in different regions of the VP7 molecule, demonstrated that all of them were recognised by the animals tested. These results provided further molecular evidence suggesting that VP7 is indeed a major immunogenic antigen ideal for BTV antibody detection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01718592
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  • 4
    Electronic Resource
    Electronic Resource
    Expression of equine morbillivirus (EMV) matrix and fusion proteins and their evaluation as diagnostic reagents (1997)
    Springer
    Archives of virology 142 (1997), S. 2269-2279 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  Full-length cDNA clones coding for the matrix (M) and fusion (F) proteins of equine morbillivirus (EMV) were isolated by RT-PCR, and expressed in Escherichia coli using two different expression systems. Western blot analysis indicated that the M and F proteins, expressed either by itself or as fusion proteins with glutathione S-transferase (GST), were insoluble and degraded after expression. Analysis of the degradation pattern of recombinant M protein suggested that the N-terminus of the matrix protein might be more stable and antigenic than the C-terminal region. Therefore a third system was used to express a truncated M protein, composed of the N-terminal amino acid residues 1–197, with a (His)6-tag attached at the N-terminus. This recombinant protein [(His)6-Mtr], was stable but was also insoluble. After one-step affinity purification under denaturing conditions, (His)6-Mtr was used to monitor the antibody response to EMV infection by Western blot and ELISA. We obtained a 100% correlation between Western blot and virus neutralisation testing although the number of positive sera available for testing was very limited, which included seven horse, two rabbit and one human sera.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050241
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  • 5
    Electronic Resource
    Electronic Resource
    Self-assembly, antigenicity, and immunogenicity of the rabbit haemorrhagic disease virus (Czechoslovakian strain V-351) capsid protein expressed in baculovirus (1995)
    Springer
    Archives of virology 140 (1995), S. 1095-1108 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Rabbit haemorrhagic disease virus (RHDV) capsid protein was expressed in a baculovirus system. Analysis of the expressed product showed that the recombinant protein, which is 60 kDa in size, was antigenic as revealed by its reactions in ELISA and Western blot with the antibodies raised against RHDV. Direct electron microscopy of the cell culture supernatant and the purified protein demonstrated that the capsid protein expressed in insect cells self-assembled to form empty virus-like particles (VLP) which are similar in size and morphology to that of native virus. These particles were immunoreactive with polyclonal anti-RHDV antibodies and with four monoclonal antibodies which recognise conformational epitopes of the virus. The results indicated that the VLPs were morphologically and antigenically indistinguishable from native virus. The recombinant VLPs induced high levels of RHDV-specific antibodies in rabbits and mice following immunisation. The immune response to the VLPs protected the rabbits following challenge with the virulent RHDV. In haemagglutination assays, the VLPs bound to human red blood cells similar to the native virus particles. The recombinant protein and or VLPs is suitable for the development of a rapid, sensitive and reliable test for detection of antibodies to RHDV and for use as a vaccine for domestic rabbits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01315418
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  • 6
    Electronic Resource
    Electronic Resource
    Monolayer behaviors of poly(hexamethylene adipamide) at the air/water interface (1995)
    Springer
    Colloid & polymer science 273 (1995), S. 16-22 
    Details
    ISSN: 1435-1536
    Keywords: π-A and μ-A isotherms ; monolayers ; air water interface ; poly(hexamethylene adipamide) ; spreading solution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Monolayer films on the neutral water substrate were obtained by spreadingN-trifluoroacetic anhydride (NTF)-modified nylon 66 or nylon 612 in chloroform solutions. Alternatively, monolayer films were obtained by spreading from nylon 66 solutions in the 3∶1 mixture of benzene (B) and phenol (P). The temperatures studied are 10.3°, 14.7°C, and 19.4°C. The isothermss of surface pressure (π), and surface moment (μ) against surface area per residue (A) were determined. The π-A isotherms of the NTF-modified nylon 66/chloroform and the nylon 66/BP were found to be an expanded type, while that of NTF-modified nylon 612/chloroform was of a condensed type. The NTF-modified nylon 66/chloroform solutions could yield well-spread films even higher concentrations than nylon 66/BP solutions. In the μ-A isotherms at 10.3° and 14.7°C, the surface moments are constant at 143 mD/residue for NTF-modified nylon 66/chloroform, and 340 mD/residue for nylon 66/BP until the surface area reaches where the π-A isotherms show a transition point. After the transition point, the surface moments for both systems drop steadily. However, the surface moment at 19.4°C shows a maximum at the transition point. Possible configuration of the nylon 66 residue in monolayer is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00655669
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  • 7
    Electronic Resource
    Electronic Resource
    Study on the properties of a polyvinylacetate film at the air-water interface (1995)
    Springer
    Colloid & polymer science 273 (1995), S. 426-430 
    Details
    ISSN: 1435-1536
    Keywords: Polyvinylacetate ; air-water interface ; surface moment ; hysteresis ; relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Isotherms of surface pressure against surface area for a polyvinylacetate (PVAc) film at the air-water interface were determined at 20.52°C. Measurements of surface moment, hysteresis, and pressure relaxation in a constant area were subsequently conducted at appropriate area regions for elucidation of the correlation of properties and conformations of PVAc film. It is concluded that the film is stable and exhibits a perfectly reversible compression in the areas larger than 13 Å2/repeat-unit but assumes three different conformations for three regions (70-42), (42-25), and (25-13) Å2/repeat-unit, respectively. Finally, a twisting chain loop model is proposed for the interpretation of hysteresis and pressure relaxation occurring in the areas near and in the collapse region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00656886
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis and properties of copolymers from 2-hydroxyethyl methacrylate-linked nonsteroidal antiinflammatory agents with methacrylic acid (1998)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 36 (1998), S. 1481-1490 
    Details
    ISSN: 0887-624X
    Keywords: ibuprofen ; ketoprofen ; naproxen ; copolymer reactivity ; thermal stability ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Three nonsteroidal antiinflammatory drugs, 2-(4-isobutylphenyl)-propionic acid (ibuprofen), 2-(3-benzoylphenyl)-propionic acid (ketoprofen), and 2-(6-methoxy-2-naphthyl)-propionic acid (naproxen), were covalently linked with 2-hydroxyethyl methacrylate (HEMA). The drug-linked HEMA (M1) (ibuprofen-linked HEMA abbreviated as HI; ketoprofen-linked HEMA as HK, and naproxen-linked HEMA as HN), were respectively copolymerized with methacrylic acid (M2), MA, to obtain macromolecular prodrugs. The compositions of the copolymers were determined by means of a 1H-NMR spectroscopy and monomer reactivity ratios were estimated using the Kelen-Tüdös linear differential equation. The reactivity ratios are: r1 = 0.101 ± 0.012, r2 = 1.071 ± 0.065 for HI-MA; r1 = 0.344 ± 0.066, r2 = 0.966 ± 0.032 for HN-MA, and r1 = 0.650 ± 0.182, r2 = 1.032 ± 0.106 for HK-MA, respectively. The monomer reactivity toward to MA radical estimated from 1/r2 values is almost same for all three monomers (1/r2 ∼ 1). The glass transition temperatures of three drug-linked homopolymers go hand in hand with the steric hindrance of three drugs, i.e., ketoprofen 〉 naproxen ≫ ibuprofen calculated the minimum energy by computer molecular modeling. © 1998 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 36: 1481-1490, 1998
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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