Isolation of intact transition protein 2 with three zinc finger motifs from boar late spermatid nuclei.
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.
Akama
K
K
Department of Chemistry, Faculty of Science, Chiba University, Japan.
Sato
H
H
Oguma
K
K
Nakano
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D006168:Guinea Pigs; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000302:isolation & purification*; D016415:Sequence Alignment; D013087:Spermatids / Q000378:metabolism* / Q000648:ultrastructure; D016335:Zinc Fingers
D009687:Nuclear Proteins