Abstract
Immunofluorescence with an antibody against a C-terminal sequence of human topoisomerase II has been performed on nuclei released from different tissues of Pisum sativum L. All the nuclei labelled and preincubation of the antibody with the corresponding immunogen peptide strongly decreased the fluorescence. The labelling pattern (particularly nucleolar) was different in quiescent and proliferating nuclei and changed during germination. In prophase nuclei, the labelling was at the periphery of the condensing chromosomes, and in metaphase chromosomes, a characteristic labelling at pericentromeric regions was found. A computer search indicated that, apart from mammalian topoisomerase II, the immunogen peptide did not match any other sequenced protein which could reasonably be present in plant nuclei. The possible relation between the antigen recognized and topoisomerase II is discussed.
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