| First Author | Ookawara T | Year | 1997 |
| Journal | Arch Biochem Biophys | Volume | 340 |
| Issue | 2 | Pages | 299-304 |
| PubMed ID | 9143334 | Mgi Jnum | J:39652 |
| Mgi Id | MGI:87006 | Doi | 10.1006/abbi.1997.9912 |
| Citation | Ookawara T, et al. (1997) Purification and subunit structure of extracellular superoxide dismutase from mouse lung tissue. Arch Biochem Biophys 340(2):299-304 |
| abstractText | The first purification of mouse extracellular superoxide dismutase (EC-SOD) and the analysis of the native enzyme are described. Mouse EC-SOD was purified from lung tissues with a high recovery (41%) and a specific polyclonal antibody against the purified enzyme was obtained. The purified enzyme had a strong affinity for, heparin and a molecular mass of 150 kDa (estimated by a gel filtration chromatography). The native mouse EC-SOD was composed of two different sizes of subunits, a M(r) of 33 and 35 kDa (determined by SDS-PAGE). The 35-kDa subunit had an interchain disulfide bond at the C-terminus and existed as a covalent dimer in the molecule, whereas the 33-kDa subunit resulted from the 35-kDa subunit by truncating its C-terminus as a posttranslational modification, with resultant loss of the interchain disulfide bond. These results suggest that the native mouse EC-SOD is a heterotetramer composed of two different dimers, with or without a covalent bond. |
