Hybridization of subunits of rat liver arginase A1 and rat kidney arginase A4.
Recombination of subunits of rat liver arginase A1 and rat kidney arginase A4 yielded a product which in polyacrylamide gel electrophoresis and DEAE-cellulose chromatography separated into five proteins with arginase activity. Proteins I and V corresponded in polyacrylamide gel-electrophoresis, DEAE-cellulose chromatography and immunological properties to the parental forms A1 and A4, respectively. Formation of five arginase hybrids proved the tetrameric structure of native arginases.
D000818:Animals; D001119:Arginase; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008297:Male; D010446:Peptide Fragments; D055503:Protein Multimerization; D051381:Rats
D010446:Peptide Fragments; D001119:Arginase