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PubMed · 14727

[Serine proteases from Bac. subtilis].

V I Palubinskas·V S Vesa·A A Glemzha·I P Beliauskaite
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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.

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Bacillus subtilisEnzyme ActivationHydrogen-Ion ConcentrationMacromolecular SubstancesMolecular WeightPeptide HydrolasesThermodynamicsEnglish AbstractJournal Article

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V I Palubinskas, V S Vesa, A A Glemzha, I P Beliauskaite. 1976. [Serine proteases from Bac. subtilis].. https://pubmed.ncbi.nlm.nih.gov/14727/

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