与单克隆抗体偶联的产生活性氧自由基的酶的选择性细胞毒性。
Selective cytotoxicity of an oxygen-radical-generating enzyme conjugated to a monoclonal antibody.
作者信息
Battelli M G, Abbondanza A, Tazzari P L, Dinota A, Rizzi S, Grassi G, Gobbi M, Stirpe F
机构信息
Dipartimento di Patologia Sperimentale, Istituto di Ematologia Lorenzo e Ariosto Seragnoli, Università di Bologna, Italy.
出版信息
Clin Exp Immunol. 1988 Jul;73(1):128-33.
Abstract
The monoclonal antibody 8A, which recognizes a human plasma cell-associated antigen, was covalently linked to xanthine oxidase in a conjugate maintaining both immunological and enzymatic properties. A significant degree of target cell lysis was obtained at an enzyme concentration that was ineffective on non-target cells and on myeloid staminal cells (CFU-GM). The cytotoxic activity was abolished by an excess of antibody, by allopurinol and by superoxide dismutase and catalase. A possible use of the conjugate for bone marrow purging in multiple myeloma patients is suggested.
摘要
识别一种人类浆细胞相关抗原的单克隆抗体8A，在保持免疫和酶活性的偶联物中与黄嘌呤氧化酶共价连接。在对非靶细胞和髓系造血干细胞（CFU-GM）无效的酶浓度下，可实现显著程度的靶细胞裂解。过量抗体、别嘌呤醇、超氧化物歧化酶和过氧化氢酶可消除细胞毒性活性。提示该偶联物可能用于多发性骨髓瘤患者的骨髓净化。
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