Sharonov B P, Lyzlova S N
All-Union Research Institute of Highly Pure Biopreparations, Pudozhskaja, Leningrad, USSR.
Biochem Int. 1989 Jul;19(1):27-35.
The structural integrity of serum proteins: albumin, immunoglobulin G, transferrin, ceruloplasmin and superoxide dismutase, and the functional activity of the latter two enzymes after their interaction with hypochlorite were studied. It was shown that the interaction between the proteins and hypochlorite resulted in protein injury and degradation of their native structure. In the case of ceruloplasmin and transferrin, a practically complete protein "dissipation" occurred, the albumin and superoxide dismutase structures being injured in a lesser degree. The inactivation of ceruloplasmin was slower than that of superoxide dismutase. The protein degradation by hypochlorite seems to be the main factor restricting the ability of the proteins to act as antiinflammatory drugs.
研究了血清蛋白(白蛋白、免疫球蛋白G、转铁蛋白、铜蓝蛋白和超氧化物歧化酶)的结构完整性,以及后两种酶与次氯酸盐相互作用后的功能活性。结果表明,蛋白质与次氯酸盐之间的相互作用导致蛋白质损伤及其天然结构的降解。就铜蓝蛋白和转铁蛋白而言,实际上发生了蛋白质的完全“消散”,白蛋白和超氧化物歧化酶的结构受损程度较小。铜蓝蛋白的失活比超氧化物歧化酶慢。次氯酸盐引起的蛋白质降解似乎是限制蛋白质作为抗炎药物发挥作用的主要因素。