ISOLATION AND CHARACTERIZATION OF MONKEY LIVER FERRITIN

Monkey liver ferritin was isolated and purified along with human liver ferritin and their physicochemical and immunological characteristics were compared. The apparent molecular weight of monkey liver ferritin was estimated to be 430 kDa as against 450 kDa of human liver ferritin . Both ferritins appeared to be made up of a 22.5 kDa polypeptide unde r denaturing conditions and the proteins contained neutral sugar (wt/w t) of 2.0% (monkey) and 2.4% (human). By immunoblots both human and mo nkey liver ferritins showed appreciable cross-reactivity with the poly clonal antibodies raised against either proteins. Monkey liver ferriti n, however, was not recognised by the human monoclonal antibody. The a mino acid composition of both ferritins was more or less similar. Isoe lectric focusing indicated that monkey liver ferritin showed microhete rogeneity with three bands at pI 5.4, 5.5 and 5.6, whereas human liver ferritin showed a single band at pI 5.6 confirming the relative acidi c nature of monkey liver ferritin.