Results 181 to 190 of about 10,158 (214)

Membrane matrix disruption by melittin

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1972
Abstract 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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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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The interaction of melittin with troponin C

Archives of Biochemistry and Biophysics, 1987
Melittin has been found to interact with troponin C with high affinity in the presence of Ca2+. The association constant approaches in magnitude that for melittin and calmodulin. The interaction results in a shift to lower wavelengths of the emission band of Trp-19 of melittin and in an increased shielding of Trp-19 from quenching.
R F, Steiner, L, Norris
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Mechanism of the conformational transition of melittin

Biochemistry, 1992
It is known that, while melittin at micromolar concentrations is unfolded under conditions of low ionic strength at neutral pH, it adopts a tetrameric alpha-helical structure under conditions of high ionic strength, at alkaline pH, or at high peptide concentrations.
Y, Goto, Y, Hagihara
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Peptide inhibitors of melittin action

Journal of Protein Chemistry, 1996
The 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, J, Werkmeister, A, Kirkpatrick, C, Curtain, G, Pantela, D E, Rivett   +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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Topology of the calmodulin-melittin complex.

Journal of molecular biology, 1998
The 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, Miraglia N, Orru S, Amodeo P, Motta A, Marino G, Pucci P   +6 more
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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-regenerated purple membrane

Biochemistry (Moscow), 2009
We have investigated the character of melittin-regenerated purple membrane. Adding melittin to blue membrane causes the color transition and partial regeneration of the photocycle and the proton pump. The reconstitution of bacteriorhodopsin by melittin is proved to be charge-dependent.
Yue, Zhang, Tao, Su, Kun-Sheng, Hu
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Melittin: An allergen of honeybee venom

Journal of Allergy and Clinical Immunology, 1977
The 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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