[Trypsin-like proteinase from Actinomyces fradiae 119].
Using electrophoresis and ultracentrifugation, a homogeneous proteinase was isolated from protofradine, a protease Act. fradiae 119 preparation. The purification procedure included filtration on DEAE-cellulose, gel filtration through Arcylex P-10, CM-chromatography and desalting on Sephadex G-15. The proteinase under study is an endopeptidase which hydrolyzes low molecular weight synthetic trypsin substrates as well as casein and denaturated collagen. Diisopropylfluorophosphate and soya bean trypsin inhibitor completely inhibit the proteinase activity, whereas pCMB and EDTA have no such effect. The stability maximum is observed at pH of 2.5-3.5, the action maximum at pH 8.7-9.5. The amino acid composition of the enzyme is similar to that of trypsin from Str. griseus. The molecular weights of the proteinase as determined by gel filtration and sedimentation equilibrium method are equal to 25400 and 26500, respectively. The isoelectric point lies at 5.3. The data obtained suggest that the proteinase can be attributed to the family of trypsin proteinases.
D000190:Actinomyces / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism*
D000596:Amino Acids; D010447:Peptide Hydrolases; D014357:Trypsin
Tripsinopodobnaia proteinaza Actinomyces fradiae 119.