Open AccessNonidentity of subunits of human kidney arginase A1 and human liver arginase A5.
Author(s) -
Zofia Porembska,
Wojciech Graboń,
E Zelazowska,
Hanna Czeczot,
E Zamecka
Publication year - 1993
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1993_4785
Subject(s) - arginase , human liver , enzyme , kidney , biochemistry , chemistry , human kidney , protein subunit , biology , microbiology and biotechnology , arginine , amino acid , endocrinology , gene
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.