Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Elastase is a serine protease which exhibits endopeptidase activity on many proteins, its principal substrate, however, is elastin and it is unique among proteases in its ability to hydrolyse native elastin. It is present in the pancreas, leukocytes and serum. Elastase consists of a single polypeptide chain with a molecular weight of 29.5kDa. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2A is secreted from the pancreas as a zymogen. In other species, elastase 2A has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues. Elastase 1 is not a pancreatic enzyme: clinical literature that describes human elastase 1 activity in the pancreas is actually referring to elastase 2A.
Elastase; ELA 1; ELA2A; ELA 2B; ELA 3; ELA 3A; ELA 3B; Fecal pancreatic elastase 1; HLE; Medullasin; Pancreatic elastase IIA; PE 1; Protease E
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