鲁米诺取代的肽和蛋白质的酶促活化与捕获。一种增强抗肿瘤抗体细胞毒性的可能方法。
Enzymatic activation and trapping of luminol-substituted peptides and proteins. A possible means of amplifying the cytotoxicity of anti-tumor antibodies.
作者信息
Parker C W, Aach R D, Philpott G W
出版信息
Proc Natl Acad Sci U S A. 1975 Jan;72(1):338-42. doi: 10.1073/pnas.72.1.338.
Glutathione and glucose oxidase (EC 1.1.3.4) conjugates containing covalently bound luminol were prepared as prototypes for peptides and proteins with latent, enzyme-activatable chemical reactivity. In the presence of small quantities of activated horseradish peroxidase, conjugated luminol molecules were oxidized to unstable free radicals which reacted rapidly with soluble proteins and cells. These observations are of interest in regard to possible sequential localization reactions in which a few molecules of cell-bound antibody-horseradish peroxidase would be used to catalytically alter and trap many molecules of a second (luminol-substituted) enzyme, toxin, or hapten in the same area, as might be desirable in promoting selective cell destruction.
制备了含有共价结合鲁米诺的谷胱甘肽和葡萄糖氧化酶（EC 1.1.3.4）缀合物，作为具有潜在酶可激活化学反应性的肽和蛋白质的原型。在少量活化辣根过氧化物酶存在下，缀合的鲁米诺分子被氧化成不稳定的自由基，这些自由基与可溶性蛋白质和细胞迅速反应。这些观察结果对于可能的顺序定位反应很有意义，在这种反应中，少量细胞结合抗体 - 辣根过氧化物酶分子可用于催化改变并捕获同一区域内许多分子的第二种（鲁米诺取代的）酶、毒素或半抗原，这在促进选择性细胞破坏中可能是理想的。
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