[Physicochemical properties of a fibrinolytic enzyme from Streptomyces thermovulgaris culture broth].
Some properties of fibrinolytic enzyme from cultural fluid of Streptomyces thermovulgaris have been studied. The molecule of enzyme has been shown to consist of one polypeptide chain with molecular mass 28000 dalton, pi = 7.45-7.6. The amino acid composition of protein is determined, the protein does not contain cysteine residues. The enzyme is not thermostable, and Ca2+ ion does not exert stabilized influence. In opposition to diisopropylfluorophosphate, phenylmethylsulfonyl fluoride does not inhibit the enzyme activity.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004591:Electrophoresis, Polyacrylamide Gel; D005342:Fibrinolysis / Q000187:drug effects*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature; D014461:Ultracentrifugation
D000596:Amino Acids; D010447:Peptide Hydrolases
Fiziko-khimicheskie svoĭstva fibrinoliticheskogo fermenta iz kul'tural'noĭ zhidkosti Streptomyces thermovulgaris.