Elastase is a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges. The molecular mass is approximately 25.9kDa. The enzyme is synthesized as an inactive zymogen, proelastase, which is converted to the active form by limited proteolysis at the N-terminal by trypsin.
Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.
Enzyme that degrades elastin, a matrix component of tissues involved in stretching processes. It is a serine protease with broad specificity. It cleaves protein at the carboxyl side of small hydrophobic amino acids such as Ile, Gly, Ala, Ser, Val, and Leu. The enzyme also hydrolyzes amides and esters such as N-Benzoyl-L-alanine methyl ester.