[Isolation of individual proteases from protofradin].
An electrophoretically homogeneous trypsin-like proteinase, two homogeneous proteases (presumably metal-containing) and two elastases, possessing the ATEE-esterase activity, were isolated from protofradin, a protease preparation from Actinomyces fradiae 119, using fractionation on KM-cellulose K-32. The trypsin like proteinase of protofradin possesses the esterase activity, equal to the activity of pancreatic trypsin. Protofradin elastases differ in their pH optima, response to EDTA, stability upon storage and the degree of elastin hydrolysis. The specificity of elastase is probably the same, since in elastin both enzymes hydrolyze the peptide bonds, formed by the NH2-group of glycine and alanine residues, found in elastin in large amounts. The end products of elastin hydrolysis are tripeptides.
[Isolation of individual proteases from protofradin]. An electrophoretically homogeneous trypsin-like proteinase, two homogeneous proteases (presumably metal-containing) and two elastases, possessing the ATEE-esterase activity, were isolated from protofradin, a protease preparation from Actinomyces fradiae 119, using fractionation on KM-cellulose K-32. The trypsin like proteinase of protofradin possesses the esterase activity, equal to the activity of pancreatic trypsin. Protofradin elastases differ in their pH optima, response to EDTA, stability upon storage and the degree of elastin hydrolysis. The specificity of elastase is probably the same, since in elastin both enzymes hydrolyze the peptide bonds, formed by the NH2-group of glycine and alanine residues, found in elastin in large amounts. The end products of elastin hydrolysis are tripeptides.