Rivero O, Anguita J, Paniagua C, Naharro G
Departmento de Patologia Animal (Sanidad Animal), Unidad de Microbiología, Facutad de Veterinaria, Universidad de León, Spain.
J Bacteriol. 1990 Jul;172(7):3905-8. doi: 10.1128/jb.172.7.3905-3908.1990.
A structural gene which codes for an extracellular protease in Aeromonas hydrophilia SO2/2 and D13 was cloned in Escherichia coli C600-1 by using pBR322 as a vector. The gene codes for a temperature-stable protease with a molecular mass of approximately 38,000 daltons. The protein was secreted to the periplasm of E. coli C600-1 and purified by osmotic shock. Cloned protease (P3) was identical in molecular mass and properties to the one purified from A. hydrophila SO2/2 culture supernatant as an extracellular product.
利用pBR322作为载体,将嗜水气单胞菌SO2/2和D13中编码一种细胞外蛋白酶的结构基因克隆到大肠杆菌C600-1中。该基因编码一种分子量约为38,000道尔顿的温度稳定蛋白酶。该蛋白分泌到大肠杆菌C600-1的周质中,并通过渗透休克法进行纯化。克隆的蛋白酶(P3)在分子量和性质上与从嗜水气单胞菌SO2/2培养上清液中作为细胞外产物纯化得到的蛋白酶相同。