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Description

Native elastase from porcine pancreas. Catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin, and of a number of synthetic substrates containing aspartic acid, glutamic acid, phenylalanine, or tyrosine. Preferentially cleaves peptide bonds at the carbonyl end of amino acid residues with small hydrophobic side chains, such as glycine, valine, leucine, isoleucine, and particularly alanine. Inhibited by DFP, elastinal, and alpha2-macroglobulin. Has an optimal pH of 7.8-8.5, pI = 9.5. Note: Elastase tends to adhere to glass. Hence, use of siliconized glassware is recommended., Native elastase from porcine pancreas. A serine protase that catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin and of a number of synthetic substrates containing aspartic acid, phenylalanine, or tyrosine. Inhibited by DFP, elastinal, and alpha2-macroglobulin.