title: Studies on proteolytic activity in commercial myoglobin preparations.
abstract: Commercial myoglobin preparations from horse skeletal muscle degraded casein. The maximum activity was at pH8-8.5. A muscle myofibril preparation was also attacked. The protease could be partly separated from the myoglobin by selective ultrafiltration through a membrane with an exclusion limit of mol.wt. 30000. A greater than 1000-fold purification of the proteolytic activity was achieved by affinity chromatography with soya-bean trypsin inhibitor bound to CM-cellulose. The enzyme preparation hydrolysed p-toluenesulphonyl-l-arginine methyl ester and N-benzyloxycarbonyl-l-tyrosine p-nitrophenyl ester. Its activity was inhibited strongly by soya-bean and ovomucoid trypsin inhibitors, serum and the soluble fraction of muscle homogenates. EDTA, p-chloromercuribenzoate and phenylmethylsulphonyl fluoride also caused some inhibition.
mesh_terms: D001120:Arginine; D002364:Caseins; D002729:Chloromercuribenzoates; D002845:Chromatography; D002846:Chromatography, Affinity; D003956:Dialysis; D004492:Edetic Acid / Q000494:pharmacology; D004952:Esters; D005374:Filtration; D005459:Fluorides; D006863:Hydrogen-Ion Concentration; D008747:Methylcellulose; D009210:Myofibrils; D009211:Myoglobin; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011480:Protease Inhibitors; D013451:Sulfonic Acids; D014020:Tissue Extracts; D014361:Trypsin Inhibitors; D014443:Tyrosine
chemical_list: D002364:Caseins; D002729:Chloromercuribenzoates; D004952:Esters; D009211:Myoglobin; D011480:Protease Inhibitors; D013451:Sulfonic Acids; D014020:Tissue Extracts; D014361:Trypsin Inhibitors; D014443:Tyrosine; D008747:Methylcellulose; D001120:Arginine; D004492:Edetic Acid; D010447:Peptide Hydrolases; D005459:Fluorides