Staphylococcal L-asparaginase: purification and properties of enzymic protein
Rózalska, M.
Acta Microbiologica Polonica 38(3-4): 233-245
1989
ISSN/ISBN: 0137-1320 PMID: 2484741 Document Number: 338611
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.