Searle F, Bier C, Buckley R G, Newman S, Pedley R B, Bagshawe K D, Melton R G, Alwan S M, Sherwood R F
Br J Cancer. 1986 Mar;53(3):377-84. doi: 10.1038/bjc.1986.62.
Carboxypeptidase G2, a zinc metalloenzyme isolated from Pseudomonas sp. strain RS-16, which catalyses the hydrolytic cleavage of reduced and non-reduced folates to pteroates and L-glutamate, has been linked to a monoclonal antibody (W14A) raised to human chorionic gonadotrophin. The coupling efficiency and retention of antibody and enzymatic activities are compared for three separate methods of preparing 1:1 conjugates. Preliminary in vitro studies on the cytotoxicity of the free enzyme and the conjugated enzyme towards JAR choriocarcinoma cells are reported. Despite the limitations of the in vitro model, it could be demonstrated that a significant proportion of 10(6) choriocarcinoma cells lost viability when exposed to either free or conjugated enzyme for 72 hours at concentrations of carboxypeptidase G2 of 1-3 units ml-1 of medium.
羧肽酶G2是一种从假单胞菌属RS-16菌株中分离出的锌金属酶,它催化还原型和非还原型叶酸水解裂解为蝶酸和L-谷氨酸,该酶已与一种针对人绒毛膜促性腺激素产生的单克隆抗体(W14A)连接。比较了三种单独制备1:1缀合物的方法的抗体偶联效率以及抗体和酶活性的保留情况。报告了游离酶和缀合酶对JAR绒毛膜癌细胞的细胞毒性的初步体外研究。尽管体外模型存在局限性,但可以证明,当在培养基中羧肽酶G2浓度为1 - 3单位/毫升的条件下,将10⁶个绒毛膜癌细胞暴露于游离酶或缀合酶72小时时,相当大比例的细胞失去了活力。