Results 161 to 170 of about 7,362 (203)

Structure and Function of Cobra Venom Factor, the Complement-Activating Protein in Cobra Venom

1996
Cobra Venom Factor (CVF) is an unusual venom component known to be present in the venom of the cobra species Naja, Ophiophagus, and Hemachatus of the Elapidae family (1). CVF is not a toxin in the classical sense. As a matter of fact, the purified molecule is not toxic.
C W, Vogel, R, Bredehorst, D C, Fritzinger, T, Grunwald, P, Ziegelmüller, M A, Kock   +5 more
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Antiproliferative Activity of Cobra Venom Cytotoxins

Current Topics in Medicinal Chemistry, 2015
Cytotoxins (or cardiotoxins, CTs) are small rigid membrane-active proteins of the three-finger toxin (TFT) family. They comprise about 60 amino acid residues, stabilized by four disulphide bridges. CTs, the most abundant proteins in cobra venom are able to kill cancer cells in a dose and time-dependent manner.
Peter V, Dubovskii, Yuri N, Utkin
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Multiple Forms of Cobra Venom Phospholipase A

Nature, 1967
MULTIPLE forms of enzymes catalysing identical reactions can exist even in one tissue1. Cobra venom is a rich source of phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4)2. This enzyme catalyses the conversion of lecithin and other phospholipids to lysophosphatides, by removal of a fatty acid residue in the second position of the phospholipid ...
B M, Braganca, Y M, Sambray
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The structural evolution of cobra venom cytotoxins

Journal of Molecular Evolution, 1987
In order to analyze the evolutionary behavior of the cobra venom cytotoxins, their probable tertiary structure was predicted using computer graphics. The 41 amino acid sequences known show that the major evolutionary changes have taken place in two particularly exposed areas of the molecular surface.
R, Breckenridge, M J, Dufton
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Use of Bromsulphalein for Assay of Cobra Venom*

Journal of the American Pharmaceutical Association (Scientific ed.), 1952
A colorimetric test is described for certain chemical constituents in cobra (Naja) venom, which are proportional to the toxic index in mice. The method consists of measuring the color intensity of an alkaline solution of the precipitate complex formed by an acid solution of Bromsulphalein with cobra venom.
G S, WARNER, J H, BREWER, H A, DUNNING
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Cobra Venom

2000
Abstract Cobra venom (Naja spp.) is a colorless, protein-rich liquid containing a complex mixture of toxic substances that are best divided into two groups. One major group has broad spectrum lytic effects on a wide range of cells, such as blood cells, muscle, and the heart (“cardiotoxins,” “lytic factor,” “cytotoxin,” “membrane ...
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Fractionation of venom from the ringhals cobra

Biochimica et Biophysica Acta, 1959
Abstract 1. 1. Venom from the South African ringhals cobra ( Hemachatus haemachates ) has been studied by chromatography on DEAE cellulose and by column electrophoresis, with special regard to the isolation and purification of certain enzymes. 2. 2.
W, BJORK, H G, BOMAN
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Studies of Immunosuppression by Cobra Venom Factor

The Journal of Immunology, 1978
Abstract The immunosuppressive activity of CVF was evaluated in mice immunized with sheep erythrocytes and dinitrophenylated proteins. Serum antibody levels to these immunogens were estimated in activity units and on a weight basis for IgG. IgM as well as IgG antibody responses were diminished in mice pretreated with CVF.
T Matsuda, G P Martinelli, A G Osler
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Neutralization of cobra venom by cocktail antiserum against venom proteins of cobra (Naja naja naja)

Biologicals, 2014
Naja naja venom was characterized by its immunochemical properties and electrophoretic pattern which revealed eight protein bands (14 kDa, 24 kDa, 29 kDa, 45 kDa, 48 kDa, 65 kDa, 72 kDa and 99 kDa) by SDS-PAGE in reducing condition after staining with Coomassie Brilliant Blue. The results showed that Naja venom presented high lethal activity.
C, Venkatesan, M, Sarathi, G, Balasubramanaiyan, S, Vimal, N, Madan, N, Sundar Raj, S, Mohammed Yusuf Bilal, A, Nazeer Basha, M A, Farook, A S, Sahul Hameed, G, Sridevi   +10 more
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COBRA VENOM.

The American Journal of the Medical Sciences, 1940
Aaron E. Parsonnet, Arthur Bernstein
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