Purification and properties of an L-asparaginase from Fusarium tricinctum |
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| Authors: | R W Scheetz H A Whelan J C Wriston |
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| Affiliation: | 1. Department. of Chemical Engineering, Polytechnic School, University of Sao Paulo, Sao Paulo, Brazil;2. Department of Biochemical-Pharmaceutical Technology, School of Pharmaceutical Sciences, University of Sao Paulo, Sao Paulo, Brazil;3. Center of Excellence in Translational Medicine (CEMT) and Scientific and Technological Bioresource Nucleus (BIOREN), Universidad de La Frontera, Temuco, Chile;4. Institute of Technical Chemistry, Faculty of Natural Science, Leibniz University Hannover, Hannover, Germany;1. Marine Biotechnology and Natural Products Extract Laboratory, National Institute of Oceanography and Fisheries, Alexandria, Egypt;2. Marine Microbiology Laboratory, National Institute of Oceanography and Fisheries, Alexandria, Egypt;1. Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, Egypt;2. Marine Biotechnology and Natural Products Extract Laboratory, National Institute of Oceanography and Fisheries (NIOF), Alexandria, Egypt;3. Biochemistry Department, College of Science, King Saud University, Bld. 5, Lab AA10, P.O. Box: 2454, Riyadh, Saudi Arabia;1. Institute of Drug Technology, Oswaldo Cruz Foundation, Rio de Janeiro, RJ, Brazil;2. Immunobiological Technology Institute, Oswaldo Cruz Foundation, Rio de Janeiro, RJ, Brazil;3. Department of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, DF, Brazil;4. Department of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, Brazil |
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| Abstract: | 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. |
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