Systemic Enzyme for Therapeutic Purposes Part 1

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It is therefore normal to use enzymes for therapeutic purposes. Substitution in intestinal enzyme deficiency conditions is a classical treatment modality that no one would dispute. External use of
enzymes for impaired wound healing (e.g. in the presence of varicose ulcers) has been part of the armamentarium of medical practitioners for centuries. Parental lytic therapy with streptolinase
or urokinase for cardiac infarct or for vascular occlusions is today standard throughout the world.

Enzymes are very highly substrate specific. Due to their different places of action, it is therefore reasonable to use mixtures of enzymes in the treatment of diseases. One important enzyme is
called the hydrolases, which cleave complex compounds (esters, peptides, and glycosides).

There are some substances that are very similar to co-enzymes. They look so similar that our body can not distinguish between them.In fact, our system does not see the difference and tries to use them as real active enzymatic centers. Of course, the enzyme compensated by such substances (not the true co-enzyme) do not work and the biochemical error makes us sick.

For example, when poisoning rats, these poisons very frequently contain an aromatic, vegetal substance known as cumarine. The animal and the human organism see the cumarine as if it were co-enzyme vitamin K. This vitamin K has a definitive role in the production of the enzymes necessary for coagulation.

If the body receives cumarine, it incorporates it into the enzymes, instead of incorporating vitamin K, and so the necessary enzymes for coagulation stop functioning. The blood liquefies in a way that causes the rats to bleed to their death.

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