title: Staphylococcal L-asparaginase: purification and properties of enzymic protein.
abstract: Staphylococcal L-asparaginase has been purified 400-fold with 40% recovery. The procedure involves ammonium sulphate precipitation and a column chromatography on Sephadex G-200 gel filtration). The enzyme is composed of not identical subunits. protein (pI 4.4) with the approximate molecular weight of 125,000 (estimated by Sephadex G-200 gel filtration). The enzyme is composed of not identical subunits. The polyacrylamide-SDS gel electrophoresis indicated two subunits with molecular weight 18,000 and 22,000.
authors.affiliation: Department of Pharmaceutical Microbiology, Academy of Medicine, Lódź, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Rózalska
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001215:Asparaginase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008970:Molecular Weight; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D001215:Asparaginase