Black mamba

Strydom (1976) performed the purification of Dendroaspis polylepis polylepis (black mamba) venom, and found 12 low molecular weight proteins, of which 11 have subcutaneous LD50 values of less than 40 vg/g mouse. 

Jouhert, F.J., Taljaard, N. (1978). The complete primary stmcture and toxin C from Dendroaspis polylepis polylepis (black mamba) venom. S. Afr. J. Chem. 31 107-10. 

Strydom, D.J. (1976). Snake venom toxins. Purification and properties of low-molecular-weight polypeptides of Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 69 169-76. 

In order to explore deeper insight into the mechanism of actions of DHPs, several authors carried out molecular modehng studies on these compounds [52-54]. In a recent molecular modeling study on calcium channel blockers, nifedipine and black mamba toxin FS2 (a venom of the black mamba snake, which has been demonstrated to block the L-type calcium channel [55,56], is a small peptide consisting of 58-74 amino acid residues and having 4-5 intramolecular disulfide bridges formed by cystein residues), Schleifer [54] observed the following ... 

Dendroaspis Jamesoni Jamesoni Common Name(s) Black Mamba... 

Several of the most poisonous snakes in the world use inhibition of AChE as their means of killing. For example the Black Mamba (Dendroapsis polx/lepis) from Africa secretes fasciculins into its venom. The fasciculins are potent AChE inhibitors and make the Black Mamba s venom amongst the most potent venoms known only 21 mg (equivalent to about three grains of salt) would be needed to kill an average sized person. Indeed, a Hospital in South Africa reported treating seven patients for Mamba bites — all of whom died within 24 hours. The symptoms associated with a Mamba bite are tetany. 

In order to maximise the toxic potential of their venoms, many snakes have several toxins in their venoms which act by different biochemical mechanisms. This is an ingenious ploy which means that more than one of the bod/s vital systems is hit by the venom so making death more certain than if only one were hit. The Black Mamba is an excellent example of a snake with multiple toxic components in its venom. In addition to the fasciculins. Mamba venom has dendrotoxins which inhibit neurotransmission by blocking the exchange of + and - ions across the neuronal membrane. This prevents passage of the nerve impulse. If the impulse is en route to the big toe the toe will be paralysed — this is certainly not life-threatening. However, if the impulse is to the pulmonary muscles, respiratory failure and death will result. The dendrotoxins from the Black Mamba are very much less toxic than the fasciculins (it would take 1.6 g to kill a person), however the combined effect of the two toxins is far more toxic than the toxicities of the individual components (this is termed synergy) which is why the Black Mamba is lethal to humans. 

The black mamba snake s venom kills by blocking the potassium channeis in the nerve cells of victims. 

Finally, venoms from different snakes from the Elapidae and Hydrophidae families also contain a cocktail of different paralytic toxins, some of which are selective for voltage-dependent Ca channels. For instance, the venom of the black mamba Dendroaspis polylepis polylepis contains a toxin termed calciseptine, which selectively blocks L-type Ca channels [6] and the venom from the green mamba D. agusticeps contains calcicludine, a toxin that acts as a potent blocker of most of the HVA Ca channels [7]. 

Figure 3. 2D correlated (COSY) spectrum of a 0,01 M DtO solution of Den-droaspis polylepis polylepis (black mamba) inhibitor K, pD 3.4, recorded at 2S°C on a Bruker HX 360 spectrometer equipped with an Aspect 2000 data system. The spectrum was recorded with quadrature detection in ca. 22 h. The spectral width is 4464.3 Hz, the data set consists of 1024 X 1024 points. The spectral resolution was improved by multiplication of the free induction decays with a phase-shifted sine-squared bell in the U-direction and by a phase-shifted sine bell in the U-direc-tion. The spectrum after symmetrization is shown. The 2D correlated spectrum visualizes the 1-coupling connectivities and allows the assignment of resonances to individual amino acid residues. (Reproduced, with permission, from Ref. 18. Copyright 1981, Academic Press.)... 

The CE/MS analysis of the venom of the snake Dendroaspis polylepis polylepis, the black mamba, is reported by Tomer and coworkers.A VG 12-250 quad-rupole equipped with a Vestec ESI source (coaxial sheath flow interface) was employed for this experiment. The sheath fluid was a 50 50 methanol 3% aqueous acetic acid solution. The CE voltage was set at -30 kV during the analysis and the ESI needle was held at -h3 kV. The CE running buffer used was 0.01 M acetic acid at pH 3.5. The APS column was flushed with buffer solution for 10 min prior to sample analysis. The snake venom was dissolved in water at a concentration of 1 mg/ml and 50 nl of the analyte solution was injected into the column. They demonstrated the existence of at least 70 proteins from this venom. 

Source From The charaterization of snake venoms using capillary electrophoresis in conjuction with electrospray mass spectronetry Black Mambas, in Electrophoresis. 

Potassium is found in the fluids of the body as the K+ ion, and its presence is essential to the operation of our nervous system. The passage of impulses along the nerves requires the flow of K+ (and Na+) through channels in the membranes of the nerve cells. Failure of this ion flow prevents nerve transmissions and results in death. For example, the black mamba snake kills its victims by injecting a venom that blocks the potassium channels in the nerve cells. 

Fas3 (formally Toxin C) D. polylepis (black mamba)... 

---