Results 241 to 250 of about 18,137 (273)
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Melittin: An allergen of honeybee venom
Journal of Allergy and Clinical Immunology, 1977The presence of serum IgE antibodies to melittin was tested by the radioallergosorbent test (RAST). Melittin, the principal protein of honeybee venom, was isolated by gel filtration on Sephadex G-75 and covalently bound to cyanogen bromide-activated microcrystalline cellulose.
B R, Paull, J W, Yunginger, G J, Gleich
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The interaction of calmodulin with melittin
Biochemical and Biophysical Research Communications, 1986Studies utilizing the interaction of melittin with the 1-106 fragment of calmodulin, the protection of calmodulin from tryptic digestion by melittin, and the interaction of the carbocyanine dye Stains-all with the calmodulin-melittin complex have indicated that complex formation of calmodulin with melittin involves the alpha-helical connecting bridge ...
C G, Caday, R F, Steiner
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Interaction of melittin with lipid membranes
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1994Interaction of melittin with lipid membranes was studied systematically with respect to its adsorption onto membranes, its effect on membrane leakage and fusion, and micellization at various melittin/lipid ratios. It was found that melittin has a strong affinity for adsorption onto lipid membranes.
S, Ohki +3 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Abstract Conformational changes in melittin during self-association were investigated by monitoring the quenching of fluorescence of the single tryptophan residue. Acrylamide and the monovalent ions, Cs + and I − , quench melittin by a diffusion-controlled, collisional mechanism, as judged by the viscosity dependence of the process.
Steven C. Quay +2 more
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Abstract Conformational changes in melittin during self-association were investigated by monitoring the quenching of fluorescence of the single tryptophan residue. Acrylamide and the monovalent ions, Cs + and I − , quench melittin by a diffusion-controlled, collisional mechanism, as judged by the viscosity dependence of the process.
Steven C. Quay +2 more
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Archives of Biochemistry and Biophysics, 1990
The (Na+ + K+)ATPase is inhibited by the bee venom polypeptide, melittin. KCl and NaCl protect the enzyme from melittin inhibition. Analysis of the K+ and Na+ protection against melittin inhibition suggested a kinetic model which was consistent with slowly reversible melittin binding, and mutually exclusive binding of melittin with K+ and Na ...
J, Cuppoletti, A J, Abbott
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The (Na+ + K+)ATPase is inhibited by the bee venom polypeptide, melittin. KCl and NaCl protect the enzyme from melittin inhibition. Analysis of the K+ and Na+ protection against melittin inhibition suggested a kinetic model which was consistent with slowly reversible melittin binding, and mutually exclusive binding of melittin with K+ and Na ...
J, Cuppoletti, A J, Abbott
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Topology of the calmodulin-melittin complex.
Journal of molecular biology, 1998The topology of the Ca2+-calmodulin-melittin ternary complex has been investigated by a combined strategy which integrates limited proteolysis and cross-linking experiments with mass spectrometric methodologies. The rationale behind the methods is that the interface regions of two interacting proteins are accessible to the solvent in the isolated ...
Scaloni A +6 more
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Enhanced IgE and IgG Anti‐Melittin Antibody Formation Induced by Heparin‐Melittin Complexes in Mice
Allergy, 1982It is known that heparin which is strongly anionic will precipitate in vitro with cationic proteins such as melittin, the principal constituent of bee venom. Our experiments indicate that mice immunized with complexes of melittin and heparin produced greater amounts of IgE and IgG antibody (to this protein) than did mice immunized with melittin along ...
L S, Kind, E, Allaway
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Conformation of the Cecropin-Melittin Hybrid, Cecropin A(1-8)-Melittin (1-18) Antibacterial Peptide
Protein & Peptide Letters, 2004Cecropin A (1-8)-Melittin (1-18) is a synthetic cecropin A-melittin hybrid peptide with leishmanicidal activity. The primary sequence of the peptide is as follows: KWKLPKKIGIGAVLKVLTTGLPALIS-NH2. 1H and 13C 2D NMR techniques were used to deduce the conformational parameters of chemical shift, 3JNHalpha coupling constants, temperature coefficients of NH
Savita, Tauro +2 more
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The actions of melittin on membranes
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1990The molecular mechanisms underlying the various effects of melittin on membranes have not been completely defined and much of the evidence described indicates that different molecular mechanisms may underlie different actions of the peptide. Ideas about the formation of transbilayer aggregates of melittin under the influence of a transbilayer potential,
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Development of D-melittin polymeric nanoparticles for anti-cancer treatment
Biomaterials, 2021Shixian Lv +2 more
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