Results 151 to 160 of about 6,599 (204)

The Anti-Leukemic Potential of Bee Venom. [PDF]

Int J Gen Med
Solanki P, Rana M, Choudhary KS, Ahuja V, Kumar V, Tyagi A.   +5 more
europepmc   +1 more source

Apamin Increases NMDA-Induced Burst-Firing of Rat Mesencephalic Dopamine Neurons

Brain Research, 1993
peer reviewedIntracellular recordings made in vitro from rat midbrain dopamine neurons showed that apamin (100 nM) did not alter the regular spontaneous firing of the neurons, but it increased the occurrence of bursts of action potentials in N-methyl-D ...
Steven W Johnson, Vincent Seutin, R A North   +2 more
exaly   +2 more sources

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A micro-radioimmunoassay for apamin

Toxicon, 1984
A radioimmunoassay is described which allows detection of quantities of apamin between 5 and 1200 fmoles (10-2400 pg) in 50 microliter aliquots. The assay requires a few milliliters of apamin antiserum diluted 10,000-20,000 times and 125I apamin at a specific radioactivity of 2000 Ci/mmole. This assay is specific for apamin.
H, Schweitz, M, Lazdunski
openaire   +2 more sources

Anti-inflammatory effects of apamin

Toxicon, 1976
Abstract The effect of apamin on inflammation induced in rats, rabbits and guinea pigs was studied. Apamin exhibited anti-inflammatory effects on serotonin and dextran oedemas provoked in the rat foot paw. The exudative reaction was inhibited in croton oil induced inflammation.
R, Ovcharov, S, Shkenderov, S, Mihailova
openaire   +2 more sources

Immunochemistry of apamin—bee venom neurotoxin—I. Radioimmunoassay with apamin and its derivatives

Molecular Immunology, 1981
Abstract Antibodies against apamin, a neurotoxic polypeptide from bee venom were raised in rabbits by immunization with apamin or apamin-BSA conjugates. 3 H-apamin or 125 I-apamin were used in radioimmunoassay with anti-apamin for the detection of the apamin antigenic site.
S V, Komissarenko, S V, Vasilenko, E G, Elyakova, E A, Surina, A I, Miroshnikov   +4 more
openaire   +2 more sources

Cooperative disulfide bond formation in apamin

Biochemistry, 1992
Apamin is being studied as a model for the folding mechanism of proteins whose structures are stabilized by disulfide bonds. Apamin consists of 18 amino acid residues and forms a stable structure consisting of a C-terminal alpha-helix and two reverse turns.
M H, Chau, J W, Nelson
openaire   +2 more sources

Binding and toxicity of apamin

European Journal of Biochemistry, 1991
The structural features of apamin, a natural octadecapeptide from bee venom, enabling binding to its receptor and the expression of toxicity in mice, have been delineated by studying the effects on binding and toxicity of chemical modifications and amino acid substitutions in synthetic analogues.
C, Labbé-Jullié, C, Granier, F, Albericio, M L, Defendini, B, Ceard, H, Rochat, J, Van Rietschoten   +6 more
openaire   +2 more sources

Preparation and pharmacokinetics of labeled derivatives of apamin

Toxicon, 1976
Abstract Apamin, the specific, centrally acting peptide neurotoxin from bee venom, was radiolabeled by different methods in order to study its in vitro and in vivo fate. Iodination of the histidyl residue resulted in a derivative of diminished toxicity whose label was partially lost within 1 week. Furthermore, it was adsorbed on to Sephadex G-25
D, Cheng-Raude, M, Treloar, E, Habermann
openaire   +2 more sources

Solid Phase Synthesis of 13-Lysine-Apamin, 14-Lysine-Apamin and the Corresponding Guanidinated Derivatives.

International Journal of Peptide and Protein Research, 1979
In order to study the importance of arginine residues 13 and 14 in apamin, the bee venom neurotoxin, four analogues, [Lys13]‐apamin, [Lys14]‐apamin, [Har4, Har13]‐apamin and [Har4, Har14]‐apamin were synthesized and tested with respect to their neurotoxicity.
exaly   +3 more sources

Recombinant and Chemical Derivatives of Apamin

European Journal of Biochemistry, 1995
The use of the colicin A lysis protein to direct the extracellular release of a fusion protein from Escherichia coli was investigated as an approach for the preparation of recombinant animal toxins. Apamin, a bee venom neurotoxin, was used as the model toxin. It is reticulated by two disulfide bridges and interacts with small conductance Ca2+‐activated
C, Devaux, M, Knibiehler, M L, Defendini, K, Mabrouk, H, Rochat, J, Van Rietschoten, D, Baty, C, Granier   +7 more
openaire   +2 more sources