Abstract

Boar intact transition protein 2, TP2, was isolated from the late spermatid nuclei by chromatography on Fractogel EMD SO3- 650 (M), and HPLCs on Nucleosil 300 7C18, Diol-120 and Chemcosorb 3C18H. CD spectroscopy study showed that TP2 underwent a small but significant zinc dependent secondary structural change. TP2, having three potential zinc finger motifs, was shown to be contain 3 atoms of zinc bound per molecule of the protein by atomic absorption spectroscopy. These results together with the amino acid sequence of TP2 suggest that TP2 is a zinc metalloprotein with three zinc finger structures.

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