Open AccessIntracellular forms ofDrosophilatopoisomerase II detected with monoclonal antibodies
Author(s) -
Gyula Hadlaczky,
Tünde Praznovszky,
József Sófi,
Andor Udvardy
Publication year - 1988
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/16.21.10013
Subject(s) - biology , polyclonal antibodies , monoclonal antibody , microbiology and biotechnology , topoisomerase , intracellular , enzyme , in vitro , biochemistry , drosophilidae , antibody , in vivo , drosophila melanogaster , genetics , gene
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.