Redmond T M, Duke E J, Coles W H, Simson J A, Crouch R K
Exp Eye Res. 1984 Apr;38(4):369-78. doi: 10.1016/0014-4835(84)90192-1.
Superoxide dismutase activity is found in the cornea of rats, dogs, rabbits and humans. A superoxide dismutase identical to the Cu-Zn enzyme is identified by biochemical and immunochemical methods in the corneal epithelium and endothelium in relative high abundance (90-100 U mg-1 protein). The enzyme quantities detected by radioimmune assay and bioactivity assay are similar, giving evidence that the enzyme present is biologically functional. Immunohistochemical techniques demonstrate the association of the enzyme with the cytoplasm of these layers. Soluble protein extracts of corneal stroma exhibit weak apparent superoxide dismutase activity which is found to be mainly due to copper associated with serum albumin.
超氧化物歧化酶活性在大鼠、狗、兔子和人类的角膜中均有发现。通过生化和免疫化学方法，在角膜上皮和内皮中鉴定出一种与铜锌酶相同的超氧化物歧化酶，其含量相对较高（90 - 100 U mg-1蛋白质）。通过放射免疫测定法和生物活性测定法检测到的酶量相似，这表明所存在的酶具有生物学功能。免疫组织化学技术显示该酶与这些层的细胞质相关。角膜基质的可溶性蛋白质提取物表现出较弱的表观超氧化物歧化酶活性，发现这主要是由于与血清白蛋白结合的铜所致。
