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Nucleic Acids Research, 1988, Vol. 16, No. 21 10013-10023
© 1988

ENZYMOLOGY

Intracellular forms of Drosophila topoisomerase II detected with monoclonal antibodies

Gyula Hadlaczky, Tünde Praznovszky, József Sófi1 and Andor Udvardy1

Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences 6701 Szeged, Hungary 1Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences 6701 Szeged, Hungary

Received August 16, 1988. Accepted September 27, 1988.

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 Orosophila 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.


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