[Intracellular proteases of Thermoactinomyces vulgaris. 2. Biochemical characterization of proteases in cell extracts].
The intracellular proteases (IP) of the cellular extract of Thermoactinomyces vulgaris are characterized as to the biochemical properties compared with the corresponding extracellular proteases (EP). According to that, the storage stability and the temperature and pH behaviour (optimum, stability) of both of the proteases are identical. Nevertheless, differences were detected between IP and EP after the action of several effectors and different substrates. As could be seen after a column chromatographic separation of the IP of the cellular extract, it is composed of at least 3 proteases, two of them are serine proteases which can be inhibited moreover unspecifically by p-chloromercuri benzoate. The purified proteases (IP) are very instable and therefore not yet characterized in detail.
D002851:Chromatography, High Pressure Liquid; D006863:Hydrogen-Ion Concentration; D008848:Micromonosporaceae / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D013307:Streptomycin / Q000494:pharmacology; D013379:Substrate Specificity; D013696:Temperature
D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D013307:Streptomycin
Intrazelluläre Proteasen aus Thermoactinomyces vulgaris. 2. Mitt. Biochemische Charakterisierung der Proteasen des Zellextraktes.