Previous studies have indicated that E. coli AS 1.357 L-asparaginase differs from that of other sources including some strains of E. coli, in both biochemical properties and conformation. A study was, therefore, under...Previous studies have indicated that E. coli AS 1.357 L-asparaginase differs from that of other sources including some strains of E. coli, in both biochemical properties and conformation. A study was, therefore, undertaken to define the chemical composition and primary structure of L-asparaginase from E. coli AS 1.357. This paper presents the amino acid composition and the amino-terminal sequence of the enzyme.展开更多
文摘Previous studies have indicated that E. coli AS 1.357 L-asparaginase differs from that of other sources including some strains of E. coli, in both biochemical properties and conformation. A study was, therefore, undertaken to define the chemical composition and primary structure of L-asparaginase from E. coli AS 1.357. This paper presents the amino acid composition and the amino-terminal sequence of the enzyme.