Nonidentity of subunits of human kidney arginase A1 and human liver arginase A5.

  • Z Porembska Department of Biochemistry, Medical Academy, Warsaw, Poland.;
  • W Grabon
  • E Zelazowska
  • H Czeczot
  • E Zamecka

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.
Published
1993-12-31
Section
Articles