V9000
Snake venom from Naja melanoleuca (Black Cobra)
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About This Item
Code UNSPSC :
12352200
Température de stockage
−20°C
Application
Snake venom from Naja melanoleuca (black forest cobra) may be used as a source of long postsynaptic neurotoxin, cardiotoxin and phospholipase A2 as well as other toxins. It may also be used as an immunogen or for proteomic research.
Actions biochimiques/physiologiques
Has high acetylcholinesterase activity
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Salwa S Seddik et al.
Journal of natural toxins, 11(4), 329-335 (2002-12-31)
This study was performed to assess the ability of polyvalent snake venom anti-serum, produced by the Egyptian Organization for Biological Products & Vaccines (VACSERA), to neutralize several toxic activities of snake venoms, not only of those included in the antivenom
J H van Eijk et al.
European journal of biochemistry, 132(1), 183-188 (1983-04-15)
Unlike porcine pancreatic phospholipase A2, the enzyme from Naja melanoleuca does not display biphasic kinetic behaviour at substrate concentrations around the critical micelle concentration. This snake venom enzyme was further investigated by direct binding studies using n-tridecylphosphocholine. Binding of this
V R Osorio e Castro et al.
Toxicon : official journal of the International Society on Toxinology, 27(5), 511-517 (1989-01-01)
Pyrularia thionin (P. thionin) is a strongly basic peptide of 47 amino acids which is hemolytic, cytotoxic and neurotoxic. It shows the greatest hemolytic activity toward human erythrocytes. Rabbit, guinea pig and pig erythrocytes show decreasing activity in that order
J H van Eijk et al.
European journal of biochemistry, 140(2), 407-413 (1984-04-16)
The fluorescent probe 8-anilinonaphtalene-1-sulfonate (ANS) binds at the active site of the Naja melanoleuca snake venom phospholipase A2, thus protecting the enzyme against active-site-directed chemical modification. Both hydrophobic and electrostatic interactions are involved in the binding. At pH 7.5, a
Elizabeth M Goebel et al.
PloS one, 4(8), e6778-e6778 (2009-08-27)
Although B. bronchiseptica efficiently infects a wide range of mammalian hosts and efficiently spreads among them, it is rarely observed in humans. In contrast to the many other hosts of B. bronchiseptica, humans are host to the apparently specialized pathogen
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