title: Nonidentity of subunits of human kidney arginase A1 and human liver arginase A5.
abstract: The main forms of arginase A1 from human kidney and A5 from human liver were purified to homogeneity. Molecular weight of both forms of enzyme approximates 120,000. In the presence of EDTA these arginases dissociate into single type distinct subunits. M(r) of both kinds of subunits is 30,000. Similarly as native arginase forms, they differ in electric charge and display complete immunological incompatibility.
authors.affiliation: Department of Biochemistry, Medical Academy, Warsaw, Poland.
authors.forename: Z
authors.initials: Z
authors.lastname: Porembska
authors.forename: W
authors.initials: W
authors.lastname: Grabon
authors.forename: E
authors.initials: E
authors.lastname: Zelazowska
authors.forename: H
authors.initials: H
authors.lastname: Czeczot
authors.forename: E
authors.initials: E
authors.lastname: Zamecka
mesh_terms: D000328:Adult; D001119:Arginase / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008875:Middle Aged; D008970:Molecular Weight; D011487:Protein Conformation; D014018:Tissue Distribution
chemical_list: D004492:Edetic Acid; D001119:Arginase