title: Glycoasparaginase in human urine.
abstract: Glycoasparaginase was purified 15,000-fold from human urine. The enzyme is a tetrameric protein of 86 kDa, composed of two heavy chains (25 kDa) and two light chains (18 kDa). Its structure and properties are very similar to those of human leukocyte glycoasparaginase. Glycoasparaginase activity is totally absent from urine of aspartylglycosaminuria patients.
authors.affiliation: Department of Clinical Chemistry, Kuopio University Central Hospital, Finland.
authors.forename: V
authors.initials: V
authors.lastname: Kaartinen
mesh_terms: D000595:Amino Acid Sequence; D001227:Aspartylglucosylaminase / Q000652:urine*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data
chemical_list: D001227:Aspartylglucosylaminase