미생물학회지 (Korean Journal of Microbiology)
- 제27권3호
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- Pages.237-244
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- 1989
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Pseudomonas carboxydovorans의 세포내 단백질 가수분해 효소의 정제 및 특징
Purification and Some Properties of an Intracellular Protease from Pseudomonas Carboxydovorans
초록
Azocasein을 기질로 사용하여 nutrient broth에서 성장한 Pseudomonas carboxydovorans로부터 다섯 단계의 순화 과정을 거쳐 68배 순화된 세포내 가용성 단백질 가수 분해 효소를 얻었다. Pyruvate나 succinate, acetate, 또는 일산화탄소를 이용하여 성장한 세균들은 이 효소의 활성을 나타내지 않았다. 순화된 효소의 크기는 약 53,000이었고, 한개의 polypeptide로 구성되어 있었다. 이 효소는 serinerp통의 단백질 가수분해 효소로
A soluble intracellular protease from cells of Pseudomonas carboxydovorans, a carboxydobacterium, grown on nutrient broth was purified 68-fold in five steps to better than 95% homogeneity with a yield of 2.4% using azocasein as a substrate. The enzyme activity was not detected from cells grown on pyruvate, succinate, acetate, or CO as a sole source of carbon and energy. The molecular weight of the native enzyme was determined to be 53,000. Sodium dodecyl sulfate-gel electrophoresis revealed the purified enzyme a monomer. The enzyme was found to be a serine-type protease. The enzyme activity was inhibited completely by several divalent cations such as