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Originally published March 1 2014

Snakes protect themselves from their own venom by producing natural chelating agent

by L.J. Devon, Staff Writer

(NaturalNews) Snake venom can be toxic to many systems of the human body. Viperine snakes will strike, inject venom and withdraw, sending haemotoxins into the blood. These toxins can also be necrotizing or deadly to the tissues. They can be anticoagulant, keeping blood from clotting. Some venom can even be neurotoxic, as seen in the Mojave rattlesnake species.

Metal ions play a powerful role in snake venom

Snake venom is loaded with various protein enzymes that act as catalysts, which speed up the chemical reaction they've instilled into their victim. Venom also contains various other elements bound to the enzymes. The powers of these elements activate the enzymes or inhibit them under certain circumstances. The metal ion enzymes in snake venom are referred to as metalloproteins. They can contain zinc ions which increase catalytic activity. They also contain calcium and magnesium ions which are required for proper substrate binding. Mercury ions can cause enzyme reactions to occur between specific enzymes, stopping enzyme inhibitors. The presence of cadmium was found to inhibit biological processes in specific enzyme activities.

How might metals like mercury affect necessary enzyme activity in the human body after one allows a viper to sink its fangs into their own blood and soft tissues?

Snake venom enzymes in action

Utilizing between 6 and 12 enzymes in their venom, snakes cause several destructive activities to occur in their victims. Some of the most common enzymes include:

Cholinesterase, which is the nervous system attacker that relaxes the muscles so the victim has very little control.

Adenosine triphosphatase is what shocks the victim and immobilizes smaller prey.

Proteases are the catalysts that disrupt tissue protein peptide, causing blood-vessel wall damage and hemorrhaging.

Amino acid oxidase
gives venom its yellow color and plays a part in digestion and the triggering of other enzymes.

Polypeptide toxins directly disrupt nerve-impulse transmission, usually causing heart or respiratory failure.

Proteolytic enzymes cause the breakdown of structural components of tissues.

Chelating agents found to inhibit biological function of snake venom, halting hemorrhage

A study conducted by researchers C. R. Goucher and H. H. Flowers used chelating agents EDTA and DTPA to observe their effects on metalloproteins from eastern cottonmouth venom.

The first observation recorded was inhibited protease activity. Protease activity is observed when the enzymes cut the peptide bonds between proteins. This stopped the venom from carrying out its own destructive biological functions. EDTA also stopped hemorrhage activity. By removing the metals from the enzymes, the chelating agents broke down the venom's destructive biological functions. When magnesium and zinc were restored in the venom enzymes, hemorrhage activity returned. When chelating agent DTPA was applied, a more powerful anti-hemorrhaging activity was observed.

This evidence shows the powerful influence that elements have on enzymes in carrying out biological functions, even destructive functions as seen in snake venom.

Snakes protect themselves from their own venom by producing natural chelating agent

An abstract, presented by researchers Francis B., Seebart C., and Kaiser II, explains how snakes generate a natural chelating agent that protects them from their own venom.

In the study, selected snake venom was studied at the molecular level for enzyme activities. The researchers found large secretions of citrate, which is produced by snakes alongside their venom. The citrate acts as a natural chelating agent, which inactivates divalent metal cations that are required for destructive biological processes of enzymes in the venom.

When the snake's citrate was applied, calcium ions were chelated, and the enzymes were found to be completely inhibited and void of venomous activity. Natural citrate secretion reduced the activity of specific enzymes, protecting the snake from its own venom. The snake practically possesses its own antivenom. This research could help medical professionals develop alternative ways to treat snakebite venom

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