1976•PubMedRequires access
[Serine proteases from Bac. subtilis].
V I Palubinskas, Vesa Vs, A A Glemzha, Beliauskaĭte Ip
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Abstract
Using biospecific adsorbent and subsequent gel-filtration of Sephadex G-75 three fractions of serine proteases (I--III) having different physicochemical properties were isolated from Bac. subtilis. The first protease had molecular weight of 23000--24000 (pH optimum 6,5, activation energy 16,6 ccal/mol. The second one had molecular weight of 29000, pH optimum 11,0, activation energy 14,4 ccal/mol. The third protease was a mixture of proteases with average molecular weights 26000 and pH optima at 7,0, 8,5 and 11,0.