Korean Journal of Microbiology (미생물학회지)
- Volume 29 Issue 3
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- Pages.167-171
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- 1991
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Purification and Characterization of an Intracellular Protease from Pseudomonas carboxydohydrogena
Pseudomonas charboxydohydrogena에서 분리 정제된 세포내 단백질 가수분해효소의 특성
Abstract
An intracellular protease from cells of Pseudomonas carboxydohydrogena grown on nutrient broth was purified to better than 95% homogeneity in five steps using azocaseine as a substrate. The molecular weight of the native enzyme was determined to be 125, 000. Sodium dodecyl sulfate-gel electrophoresis revealedat least two non-identical subunits of molecular weight 70, 000 and 56, 000. The enzyme activity was completely ingibited by phenylmethylsulfonyl fluoride and diisopropyl fluorophosphate. The enzyme was also inhibited by