Results 231 to 240 of about 18,137 (273)

Über Melittin, XI. Drei Melittine im Bienengift

Justus Liebigs Annalen der Chemie, 1972
AbstractAus 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: from honeybees to superbugs

Applied Microbiology and Biotechnology, 2019
The emergence of antibiotic-resistant bacteria, dubbed superbugs, together with relative stagnation in developing efficient antibiotics has led to enormous health and economic problems, necessitating the need for discovering and developing novel antimicrobial agents. In this respect, animal venoms represent a rich repertoire of pharmacologically active
Hamed Memariani, Mojtaba Memariani, Mohammad Shahidi-Dadras, Soheila Nasiri, Maziar Mohammad Akhavan, Hamideh Moravvej   +5 more
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Melittin interactions with adenylate cyclase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1977
Melittin, 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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Comparison between complement and melittin hemolysis: anti-melittin antibodies inhibit complement lysis

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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Structure-immunogenicity relationship of melittin, its transposed analogues, and D-melittin.

The Journal of Immunology, 1994
Abstract 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, Wade D, Coscia MR, Mitchell S, Kochoumian L, Merrifield B   +5 more
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Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced by melittin and [Ala-14]melittin

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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Characterization of Melittin Effects in Synaptosomes

Neurochemical Research, 1997
The effects of melittin at increasing concentrations on: [3H]GABA release from mouse brain synaptosomes; on the radioactivity released from [3H]arachidonic acid labeled synaptosomal membranes; on synaptosomes ultrastructure and on the leakage of the cytoplasmic marker, lactate-dehydrogenase (LDH) was investigated.
L, González, V, Nekrassov, A, Castell, M, Sitges   +3 more
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Interactions of 2,2,2‐trifluoroethanol with melittin

Magnetic Resonance in Chemistry, 2009
AbstractMelittin dissolved in 42% trifluoroethanol‐water at pH 2 has been shown to be α‐helical between residues 6 and 12 and between residues 13 and 25, with the two helical regions separated by a bend at the Leu13 residue. The inter‐helix angle was found to be 154 ± 3° at 0 °C and 135 ± 3° at 25 °C.
Robert C, Neuman, John T, Gerig
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Acyl carrier protein interacts with melittin

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1990
Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide from bee venom. ACP is a small (Mr 8847), acidic, Ca2(+)-binding protein, which possesses some characteristics resembling those of regulatory Ca2(+)-binding proteins including interaction with melittin. Complexing between melittin and ACP
Ernst-Fonberg, Mary L., Williams, Sande G., Worsham, Lesa M.S.   +2 more
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Melittin-Binding of Troponin C

The Journal of Biochemistry, 1993
Ca(2+)-dependent interaction between skeletal muscle troponin C and a bee venom melittin, which can be regarded as a mimic of the troponin C-binding peptide of troponin I, was investigated. Sephadex gel chromatography revealed that melittin bound to troponin C irrespective of the presence or absence of Ca2+ in 50 mM KCl and 50 mM Tris-HCl, pH 7.5.
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