Subunit Structure of Human Superoxide Dismutase

Subunit structure of human superoxide dismutase.

A subunit structure for human superoxide dismutase has been demonstrated by sedimentation equilibrium, agarose gel filtration, and sodium dodecyl sulfate polyacrylamide gel electrophoretic studies. This protein appears to be composed of 2 subunits, not linked by covalent bonds, each with a molecular weight about 16,000. Dissociation of the subunits is facilitated by alkylation of the two sulfhy...

Human Erythrocyte Superoxide Dismutase Encapsulated in Positively Charged Liposomes

      Superoxide dismutase (SOD) is an important antioxidant that protects many types of cells from the free radical damage. One of the possible ways for the use of SOD is its incorporation in liposomes. The aim of this study was to investigate the effect of cationic phospholipids on the entrapment of human erythrocyte superoxide dismutase (Cu/Zn SOD) in liposomes. Also, in the present study, w...

Superoxide dismutase Superoxide dismutase

Bovine erythrocyte superoxide dismutase. Subunit structure and sequence location of the intrasubunit disulfide bond.

The subunit assembly of bovine erythrocyte superoxide dismutase has been studied, through analysis of the effects of heat, removal of metal ion cofactors, and disulfide bond reduction, upon the dissociation of the subunits. Investigations utilizing sodium dodecyl sulfate-acrylamide gel electrophoresis and sedimentation equilibrium analysis demonstrate that the 2 polypeptide subunits of the prot...

Nickel superoxide dismutase structure and mechanism.

The 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site. NiSOD is a hexameric assembly of right-handed 4-helix bundles of up-down-up-down topology with N-terminal hooks chelating the active site Ni ions. This newly identified nine-residue Ni-hook structural motif (His-Cys-X-X-Pro-Cys-Gly-X-Tyr) provides almost all ...