Open AccessBeef‐Liver Arginase
Author(s) -
Harell Daniela,
Sokolovsky Mordechai
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01673.x
Subject(s) - arginase , sedimentation equilibrium , ultracentrifuge , chemistry , urea , ornithine , arginine , biochemistry , enzyme , chromatography , electrophoresis , amino acid , molecular mass , sedimentation coefficient
A procedure is described for the purification of arginase from extracts of beef liver. The enzyme which catalyzes the cleavage of L‐arginine to ornithine and urea has been purified 630‐fold, appeared to be homogeneous in the ultracentrifuge and by disc electrophoresis. The molecular weight determined by sedimentation equilibrium and amino acid analysis is 115000 ± 5000. Beef liver arginase is a slightly acidic protein ( pI 5.9) and binds 4 atom of Mn 2+ which are essential to the enzymic activity. The enzyme requires also the presence of manganese ions for stability.