GLORIA

GEOMAR Library Ocean Research Information Access

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1990-1994  (8)
Document type
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    A reference hypernetted-chain equation for soft potentials. Atomic and molecular Lennard-Jones systems (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 2724-2732 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: A recently proposed reference hypernetted-chain equation based on a semiphenomenological bridge function due to Verlet is reformulated for atomic and molecular Lennard-Jones liquids. In this new approximation we treat the size of the reference-system hard particles as a function of density and temperature through a functional relationship presented herein. The theory yields excellent results for the structure and thermodynamics of atomic Lennard-Jones liquids over a wide range of temperature and density and is quite satisfactory for Lennard-Jones homonuclear diatomics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.463062
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    On the use of semiphenomenological closures in integral equations for classical fluids (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 96 (1992), S. 6132-6137 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We have studied two choices of semiphenomenological closures for the Ornstein–Zernike equation, both for a monoatomic Lennard-Jones fluid and a dipolar homonuclear hard diatomic fluid. One of the closures was originally proposed by Verlet for hard-sphere systems, for which is known to yield good results. A second closure is proposed by us in the frame of the reference hypernetted chain (RHNC) theory. We have described the reference systems in this closure by means of Verlet's approximation and its recent extension to systems of nonspherical particles. This second approach, which we denote by RHNC-VM (Verlet's modified), turns out to give an excellent description of the structure and thermodynamics of the Lennard-Jones fluid and very accurate predictions for the structure of the dipolar diatomic system. In this latter case the apparent superiority of hypernetted chain results for configurational energies is found to stem from fortuitous cancellation of errors in the integration of the components of the pair correlation function. Nonetheless, an approximation for the bridge function capable of accounting for the particular dielectric behavior of the dipolar diatomic fluid is still lacking.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.462656
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Hypernetted and reference hypernetted chain integral equations for Lennard-Jones diatomic fluids with quadrupolar interactions (1993)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 98 (1993), S. 6465-6471 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The hypernetted chain and reference hypernetted chain integral equations are solved for quadrupolar two-center Lennard-Jones fluids and the computed fluid structure and thermodynamics are contrasted with computer simulation. A reference bridge function is determined through an empirical modification of Verlet's approximation. The resulting reference hypernetted chain equation leads to good agreement with simulation data. On the contrary, the bare hypernetted chain approximation performs poorly, in particular as far as the equation of state is concerned, which is a well-known drawback of this closure when short ranged repulsive potentials come into play.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.464811
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Integral equation and simulation studies of a realistic model for liquid hydrogen chloride (1994)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 100 (1994), S. 1599-1605 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Liquid hydrogen chloride is modeled by a system of heteronuclear two-center Lennard-Jones particles with embedded point dipoles and quadrupoles. The effect of molecular polarizability is incorporated via an effective dipole approximation. The study is performed by Monte Carlo reaction field simulation and by hypernetted chain and reference hypernetted chain integral equations. Our simulation results yield dielectric properties in excellent agreement with experimental data for liquid HCl. As for the integral equation approach, we have experimented with an empirical choice of the reference system in the spirit of a recently proposed treatment which has proved extremely successful for pure and quadrupolar two-center Lennard-Jones fluids. The hypernetted chain equation performs slightly better when accounting for the multipolar contributions to the configurational energy, but as a whole the reference hypernetted chain equation, as introduced, here proves to be a more appropriate choice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.466586
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    cDNA sequence analysis of the main olive allergen, Ole e I (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 24 (1994), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Olea europaea (Ole e) I-specific cDNA sequences were amplified by 3′-RACE-PCR, using specific primers based on the N-Terminal sequence of the allergen, and cloned into appropriate vectors. The nucleotide sequence data obtained revealed the presence of isogenic variation in Ole e I gene(s). The molecular mass, pI, amino acid composition and sequence of the predicted polypeptides agree with data previously obtained by analysis of purified Ole e I from pollen. Furthermore, by treatment of purified Ole e I with specific glycopeptide hydrotases it has been demonstrated the presence of N-glycosylation in the allergen, and there is a unique concensus site for N-Linked glycosylation at positions 111-113 of the deduced amino acid sequence. The Ole e 1 predicted sequence shows a significant homology with three putative proteins encoded respectively by the anther-specific LAT52 gene from tomato and the pollen specific genes Zmcl3 from maize and OSPSG from rice, suggesting that these proteins could have a role in one of the development processes unique to male gametophytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1994.tb00988.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    The main allergen of Olea europaea (Ole e I) is also present in other species of the oleaceae family (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 23 (1993), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Three major pollen allergens from Fraxinus excelsior, Ligustrurn vulgare and Syringa vulgaris belonging to the Oleaceae family were purified. Monoclonal antibodies previously raised against the main allergen of Olea europaea (Ole e I) were used for their purification by affinity chromatography. The three new purified allergens were able to bind human IgE from serum of olive-allergic patients in a way analogous to Ole e I. Crossed radioimmunoelectrophoresis of the four allergens, using anti-olive extract rabbit serum, showed a unique immunoprecipitation arc with the same characteristics. The four purified proteins had similar molecular weights on SIX-PAGE and the N-terminal sequences for the first 20 amino acids were identical. Furthermore, the concentration of the allergens could be determined using a two-site solid phase assay previously developed for the allergen Ole e I. Our results indicate that the four purified proteins share, to a great extent, antigenic and allergenic epitopes leading to cross-reactivities which could cause common clinical manifestations. We propose for the newly purified allergens the nomenclature of Fra e I, Lig v I and Syr v I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1993.tb00328.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Presence of IgG4 on the membrane of human basophils. Histamine release is induced by monoclonal antibodies directed against the Fab but not the Fc region of the IgG4 molecule (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 22 (1992), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We have studied the possible role of human IgG4 as an anaphylactic antibody. For that purpose, we have determined the induction of histamine release (HR) from human basophils by anti-IgE and anti-IgG4 monoclonal antibodies (MoAbs) recognizing different epitopes located at the Fe and Fab regions of the IgG4 molecule. The results show that anti-IgG4 (Fab) MoAb was able to induce HR in 93% of donors tested, with no differences between atopics and non-atopics. That HR is calcium dependent and is accompanied by the synthesis and release of leukotriene C4. In contrast, no HR could be induced by anti-IgG4(Fc) MoAbs in any individual, even in the presence of D2O or after a second challenge with a polyclonal goat anti-mouse IgG antibody. The results obtained suggest the presence of IgG4 on the basophil membrane and that the epitope recognized by the anti-IgG4 (Fc) MoAbs is probably hidden in cell-bound IgG4. This was demonstrated by immunofluorescence techniques: IgG4 bound to the basophil membrane could be detected with anti-IgG4(Fab) but not with anti-IgG4(Fc) MoAbs. In addition, we found that nine donors were unresponsive to an anti-IgE stimulus, while they released histamine efficiently after challenge with anti-IgG4(Fab), suggesting the existence of different receptors for both immunoglobulins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1992.tb03029.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Epitope mapping of the cat (Felis domesticus) major allergen Fel d I by overlapping synthetic peptides and monoclonal antibodies against native and denatured Fel d I (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Allergy 48 (1993), S. 0 
    Details
    ISSN: 1398-9995
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The major cat allergen Fel d I is a homodimer of which each monomer consists of two disulfide-linked polypeptide chains: chain 1 (70 amino acid residues) and chain 2 (92 amino acid residues). Twenty-one synthetic peptides of 14 amino acid residues length, overlapping by seven residues and spanning the entire sequence of both chains, were synthesized. These peptides were coupled to CNBr-activated Sepharose-4B and used as solid-phase antigens in epitope-mapping studies with monoclonal antibodies against native and reduced/alkylated Fel d I.Two monoclonal antibodies directed against reduced/alkylated chain I bound to the overlapping peptides 53–66 and 60–70 of chain 1. The monoclonal antibody directed against reduced/alkylated chain 2 bound to the overlapping peptides 36–49 and 43–56 of chain 2. Binding specificity was demonstrated by inhibition by reduced/alkylated Fel d I for all three monoclonal antibodies.Another monoclonal antibody against reduced/alkylated Fel d I had been found to bind predominantly to reduced/alkylated chain 2 on immunoblot in previous studies (27). It bound to peptides 1–16 and 60–70 of chain 1 and peptides 1–14 and 50–63 of chain 2; it is therefore probably directed against a conformational epitope formed by these four regions. Possibly because of low affinity of this monoclonal antibody, specificity of its binding could not be verified by inhibition studies.A panel of monoclonal antibodies directed against native Fel d I bound to peptides 1-16 and 60–70 of chain 1 and peptides 1–14 and 43–56 of chain 2. For two monoclonal antibodies, binding to each peptide was investigated and shown to be inhibitable by native Fel d I. These antibodies are therefore probably directed against a conformational epitope formed by these four regions.These studies give us substantial information about the quaternary structure of Fel d I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1398-9995.1993.tb00725.x
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...