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Collagenases from Worthington Biochemical Corporation*
Bacterial collagenase is a crude complex containing a collagenase more accurately referred to as clostridiopeptidase A which is a protease with a specificity for the X-Gly bond in the sequence Pro-X-Gly-Pro, where X is most frequently a neutral amino acid. Such sequences are often found in collagen, but only rarely in other proteins. While many proteases can hydrolyze single-stranded, denatured collagen polypeptides, clostridiopeptidase A is unique among proteases in its ability to attack and degrade the triple-helical native collagen fibrils commonly found in connective tissue.
Purified clostridiopeptidase A alone is usually inefficient in dissociating tissues due to incomplete hydrolysis of all collagenous polypeptides and its limited activity against the high concentrations of non-collagen proteins and other macromolecules found in the extracellular matrix. The collagenase most commonly used for tissue dissociation is a crude preparation containing clostridiopeptidase A in addition to a number of other proteases, polysaccharidases and lipases. Crude collagenase is well suited for tissue dissociation since it contains the enzyme required to attack native collagen and reticular fibers in addition to the enzymes which hydrolyze the other proteins, polysaccharides and lipids in the extracelluar matrix of connective and epithelial tissues.
* Text is quoted from the Worthington Enzyme Manual
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