Results 181 to 190 of about 15,825 (230)
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Molecular parameters in melittin immunogenicity
Journal of Peptide Science, 1997Based on immunogenicity studies, two T-cell epitopes in melittin were found to be functional in guinea pigs, one being centrally located, the other one residing in the C-terminal chain. In Balb/c mice only the central epitope was found to be active. A human T-cell clone was found by T-cell proliferation studies to employ strictly the C-terminal chain ...
V, Curcio-Vonlanthen +4 more
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Picosecond fluorescence spectrochronography of protein melittin and melittin-membrane complexes
Journal of Molecular Structure, 1990Abstract The results are presented of the study of protein melittin structure and dynamics when incorporated into the phospholipid bilayer carried out by time-resolved fluorescence spectroscopy with laser UV ps-pulse excitation.
A.Yu. Chikishev +3 more
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Peptide inhibitors of melittin action
Journal of Protein Chemistry, 1996The sequence of peptides necessary to inhibit melittin-induced lysis was studied using 13 peptide analogues of the inhibitor Ac-IVIFDC-NH2. Although this inhibitor is a disulfide-linked dimer, inhibition was equally effective if the thiol SH was blocked or replaced by methionine or lysine.
D, Hewish +5 more
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Membrane matrix disruption by melittin
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1972Abstract Electron spin resonance spectroscopy was used to examine the interaction of the lytic polypeptide, melittin, with model membrane systems in order to determine the physical basis for its alterations of membrane properties. Sonically dispersed egg lecithin (phosphatidylcholine), phosphatidylserine, extracted Escherichia coli phospholipids, and
J C, Williams, R M, Bell
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The Journal of Membrane Biology, 1985
This paper describes experiments designed to explore interactions between human red blood cell membranes and melittin, the main component of bee venom. We found that melittin binds to human red cell membranes suspended in isotonic NaCl at room temperature, with an apparent dissociation constant of 3 X 10(-8) M and maximum binding capacity of 1.8 X 10(7)
M T, Tosteson +3 more
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This paper describes experiments designed to explore interactions between human red blood cell membranes and melittin, the main component of bee venom. We found that melittin binds to human red cell membranes suspended in isotonic NaCl at room temperature, with an apparent dissociation constant of 3 X 10(-8) M and maximum binding capacity of 1.8 X 10(7)
M T, Tosteson +3 more
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Über Melittin, XI. Drei Melittine im Bienengift
Justus Liebigs Annalen der Chemie, 1972AbstractAus Bienengift wird durch Gelfiltration und Chromatographie über einen Kationenaustauscher (CM‐Cellulose) Melittin (einheitlicher Gipfel) eluiert. Mittels Elektrophorese auf Cellogel (Cellulose‐acetat) wird das chromatographierte Melittin in mindestens 3 Komponenten aufgespalten. Die Methode ist einfach und gut reproduzierbar.
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Melittin interactions with adenylate cyclase
Biochimica et Biophysica Acta (BBA) - General Subjects, 1977Melittin, a basic polypeptide from bee venom, inhibits basal and thyrotropin-stimulated adenylate cyclase of beef thyroid membranes with a Ki approximately 10 micron. Although this property resides in the basic C-terminal and not the N-terminal portion of the molecule, inhibition is due primarily to its detergent-like nature rather than charge effects.
G H, Cook, J, Wolff
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Biochemistry, 1988
A comparison is made between the hemolytic actions of melittin and the ninth component of complement (C9). Melittin and C9 produce "pores" of similar effective radius in erythrocytes under standardized conditions, and their hemolytic action is suppressed by metal ions at similar concentrations, suggesting a common mechanism.
R O, Laine, B P, Morgan, A F, Esser
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A comparison is made between the hemolytic actions of melittin and the ninth component of complement (C9). Melittin and C9 produce "pores" of similar effective radius in erythrocytes under standardized conditions, and their hemolytic action is suppressed by metal ions at similar concentrations, suggesting a common mechanism.
R O, Laine, B P, Morgan, A F, Esser
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Structure-immunogenicity relationship of melittin, its transposed analogues, and D-melittin.
The Journal of Immunology, 1994Abstract Melittin, a 26-residue bee venom peptide, is known to induce murine Abs specific for its hydrophilic C-terminus of residues 20×26 and T cell responses specific for its hydrophobic mid-region of residue 11-19. Synthetic melittin analogues with transposed sequences of Ac(21×26) (1×20) and Ac(26×21) (1×20) are found to induce ...
King TP +5 more
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1991
The properties of melittin and a synthetic analogue, [Ala-14]melittin (P14A), in inducing reversible transitions between vesicles and micelles at the liquid-crystalline to gel phase transition temperature (Tm) in complexes with saturated phosphatidylcholines has been studied by deuterium NMR and freeze-fracture electron microscopy (EM).
Dempsey, CE, Sternberg, B
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The properties of melittin and a synthetic analogue, [Ala-14]melittin (P14A), in inducing reversible transitions between vesicles and micelles at the liquid-crystalline to gel phase transition temperature (Tm) in complexes with saturated phosphatidylcholines has been studied by deuterium NMR and freeze-fracture electron microscopy (EM).
Dempsey, CE, Sternberg, B
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