Elastase

Elastases are enzymes in mammals, which can cleave peptide bonds, so-called proteases. Within the serine proteases to form a sub-family, which is closely related to chymotrypsin. Several, but not all elastases are able to digest elastin, an endogenous protein structure, from which the name of the group was created. When people are currently nine enzymes known to be counted among the elastases.

Elastases are proteins with 250-270 amino acid residues.

The elastases are an important part of the human immune response to pathological Gram -negative bacteria in the lungs, the gastrointestinal tract, but also to wounds. Cleave peptide bonds on the carboxy side of small hydrophobic amino acids such as glycine, alanine and valine. But your action is so non-specific that this also body's own tissue is compromised and it pathological in pneumonia and arthritis plays a role. There exist in the body several elastase Hemmproteine ​​, including α1 - antitrypsin, SLPI, elafin and alpha -2- macroglobulin. Could previously be made synthetically a few inhibitors of the protein for use in severe lung disease. Many plant substances, especially from the sunflower family ( Asteraceae), show an inhibitory effect on elastase, including flavonoids and their metabolites, caffeic acid derivatives, Triterpenabkömmlinge and sesquiterpene lactones. Up to 500 mg elastase are converted in the body every day.

Elastases of the human

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