Romanova T V, Kotova S A, Amerik A Iu, Lykov I P, Ginodman L M, Antonov V K
Bioorg Khim. 1994 Feb;20(2):114-25.
Homogeneous preparations of the ATP-dependent La proteinase from E. coli and two its mutant forms, containing an alanine residue instead of Ser679 or Ser368, were isolated. Ser679 was shown to be catalytically active rather than Ser368 as suggested in the literature. To choose between the alternative structures of the gene lon La proteinase fragments within the controversial regions were analysed and the gene structure established at the Laboratory of Proteolytic Enzymes (Institute of Bioorganic Chemistry) was confirmed. Inactivity of La proteinase in some in vitro systems suggests its functioning in vivo to be not autonomous, requiring additional factors.
从大肠杆菌中分离出了ATP依赖型La蛋白酶的均一制剂及其两种突变形式，这两种突变形式含有丙氨酸残基而非文献中所提示的Ser679或Ser368。结果表明，Ser679具有催化活性，而不是文献中所认为的Ser368。为了在有争议区域内的基因lon La蛋白酶片段的两种结构之间做出选择，对其进行了分析，并证实了蛋白水解酶实验室（生物有机化学研究所）所确定的基因结构。La蛋白酶在某些体外系统中的无活性表明其在体内的功能并非自主的，而是需要其他因子。
