title: The purification and properties of the L-serine O-sulphate degrading system of pig liver.
abstract: 1. The enzyme system from pig liver responsible for the alphabeta-elimination of l-serine O-sulphate was purified 1000-fold. 2. Isoelectric focusing produced two enzymically active fractions with isoelectric points at pH5.6 and 5.9 respectively. 3. Osmometry and gel filtration showed both enzymes to possess molecular weights of approx. 54000. 4. The separate activities exhibited similar amino acid compositions.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004798:Enzymes / Q000302:isolation & purification; D005971:Glutamates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009997:Osmotic Pressure; D012694:Serine / Q000378:metabolism*; D013431:Sulfates / Q000378:metabolism*; D013552:Swine
chemical_list: D000596:Amino Acids; D004798:Enzymes; D005971:Glutamates; D013431:Sulfates; D012694:Serine