Hadlaczky G, Praznovszky T, Sófi J, Udvardy A
Biological Research Center, Hungarian Academy of Sciences, Szeged.
Nucleic Acids Res. 1988 Nov 11;16(21):10013-23. doi: 10.1093/nar/16.21.10013.
We developed monoclonal antibodies against Drosophila topoisomerase II and studied the intracellular forms and the in vivo and in vitro proteolytic degradation of the enzyme. In purified enzyme preparations polyclonal sera and monoclonal antibodies recognized several polypeptides in the 170-132 kD molecular weight range. In vivo, however, the pattern was much simpler. In Drosophila embryos, pupae, fly heads and Schneider S3 tissue culture cells topoisomerase II appeared as a single 166 kD polypeptide. In Drosophila embryos, with two monoclonal antibodies topoisomerase II appeared as a doublet composed of the 166 kD canonical form and a slightly higher molecular weight polypeptide. Topoisomerase II was shown to be present also in fly heads which are composed entirely of nonproliferative tissues.
我们制备了针对果蝇拓扑异构酶II的单克隆抗体，并研究了该酶的细胞内形式以及其在体内和体外的蛋白水解降解过程。在纯化的酶制剂中，多克隆血清和单克隆抗体识别出分子量在170 - 132 kD范围内的几种多肽。然而，在体内，情况要简单得多。在果蝇胚胎、蛹、蝇头和施耐德S3组织培养细胞中，拓扑异构酶II表现为单一的166 kD多肽。在果蝇胚胎中，用两种单克隆抗体检测时，拓扑异构酶II表现为双峰，由166 kD的标准形式和分子量略高的一种多肽组成。拓扑异构酶II也存在于完全由非增殖组织构成的蝇头中。
