[Substrate specificity of enzymes from Bacillus mesentericus].
The proteolytic enzymes of the sporogenous Bacillus mesentericus strains 64 and 8 were tested for their ability to hydrolyse different protein substrates. The enzymes were isolated using affinity chromatography on bacillichine-silochrome, and eluted with 25% isopropanol in 0.05 M Tris-HCl buffer, pH 8.0-8.4, containing 0.01 M CaCl2. Casein, hemoglobin, elastin, albumin and synthetic peptides, Z-L-Ala-Ala-Leu-pNa and Z-L-Ala-Gly-Leu-pNa, were used as substrates. The activity of esterase was assayed in terms of indophenyl acetate cleavage. The proteinases were compared with terrilytin, a commercial preparation. The proteinase of strain 64 was active in the hydrolysis of casein, hemoglobin and elastin; its specificity was close to that of terrilytin. The proteinase of strain 8 differed from them in a higher thrombolytic and fibrinolytic activity, and had a high esterase activity.
Nesterova
N G
NG
Cherkesova
G V
GV
Kirillova
N F
NF
D000681:Amylases / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology*; D001798:Blood Proteins / Q000378:metabolism; D004338:Drug Combinations / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D005342:Fibrinolysis; D006801:Humans; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000378:metabolism; D013379:Substrate Specificity
D001798:Blood Proteins; D004338:Drug Combinations; C009402:amylase, phosphates, proteases drug combinations; D000681:Amylases; D010450:Endopeptidases; D010447:Peptide Hydrolases
Substratnaia spetsivichnost' fermentov Bacillus mesentericus.