Purification and properties of an l-asparaginase from Fusarium tricinctum

An l-asparaginase ( l-asparagine amidohydrolase, EC 3.5.1.1) from the Deuteromycete Fusarium tricinctum, has been purified to apparent homogeneity. The amino acid composition, approximate molecular weight, and certain other properties have been established. In contrast to the l-asparaginase from E. coli B, this enzyme does not appear to cause regression of the Gardner lymphosarcoma in mice. The enzyme does not hydrolyze l-glutamine, contains both galactosamine and glucosamine, and is rapidly cleared from the circulation of the mouse.