Bovine Erythrocyte Superoxide Dismutase

Zinc(II) binding to apo-(bovine erythrocyte superoxide dismutase).

The binding of zinc(II) ions to apo-(bovine erythrocytes superoxide dismutase) was studied by 1H n.m.r. spectroscopy. Two zinc(II) ions bind to each subunit of the apoenzyme, and the first has a binding constant at least an order of magnitude larger than the second. The nature of the spectral changes that occur on binding the first zinc(II) ion are interpreted in terms of a change in the struct...

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...

Action of Bovine Superoxide Dismutase

Further characterization of human erythrocyte superoxide dismutase.

1. A simplified procedure for the preparation of highly purified human superoxide dismutase from erythrocytes was developed which avoided extremes of pH and ionic strength and the use of organic solvents; the properties of human and bovine proteins, prepared by the method, were compared. 2. Using the two dimensional electrophoretic procedure of O'Farrell, the human superoxide dismutase was foun...

On the Stability of Bovine Superoxide Dismutase

1. Apo-superoxide dismutase was more labile toward a variety of inactivating stresses than was the holoenzyme. 2. cu++ restored catalytic activity to the apoenzyme and markedly enhanced its thermal stability but Cu++ plus Zn++ were needed to attain the stability of the native enzyme. 3. Co’-+ or Hgii were able to replace Zn++ in increasing the thermal stability of the Cu+f-repleted apoenzyme. I...