Purification and properties of the manganese superoxide dismutase from the liver of bullfrog, Rana catesbeiana

Abstract

A manganese Superoxide dismutase (Mn-SOD) from the liver of bullfrog, Rana catesbeiana, was purified to electrophoretic homogeneity. The enzyme has a molecular weight of about 84,000 and is composed of four identical subunits, each containing one manganese atom. The amino acid composition of the enzyme is similar to that of Mn-SODs isolated from human and chicken livers, but differs considerably from that of the Escherichia coli enzyme ( D. Barra et al. (1984) J. Biol. Chem. 259, 12595–12601; R. A. Weisiger and I. Fridovich (1973) J. Biol. Chem. 248, 3582–3592; H. M. Steinman (1978) J. Biol. Chem. 253, 8708–8720). The N-terminal amino acid is lysine. The sequence of 23 amino acid residues in the N-terminal region was determined. It shows excellent homologies with those of the human and chicken enzymes ( H. M. Steinmam and R. L. Hill (1973) Proc. Natl. Acad. Sci. USA 70, 3725–3729; C. Ditlow et al. (1982) Carlsberg Res. Commun. 47, 81–91). The frog liver enzyme is located exclusively in the mitochondrial matrix. Immunologically the same enzyme is also found in the tadpole liver, in an amount of about one-half of that in the adult bullfrog.