Isolation of intact transition protein 4 from boar late spermatid nuclei.
Boar transition protein 4 was extracted with acid from the late spermatid nuclei, and separated from the transition protein-degrading proteases by ion-exchange chromatography on Fractogel EMD SO3- 650 (M). The transition protein was further purified by HPLCs on Nucleosil 300 7C18 and Diol-200. The circular dichroic spectra of the protein with and without dithiothreitol showed that the protein had beta-form predominantly. Although sodium dodecyl sulfate affected the tertially structure of the protein, the beta-form was well retained. These indicate that the protein has a structure-forming potential for the beta-structure.
Akama
K
K
Department of Chemistry, Faculty of Science, Chiba University, Japan.
Ichimura
H
H
Kosuge
M
M
Sato
H
H
Yamaoka
Y
Y
Nakano
M
M
Tobita
T
T
D000818:Animals; D002458:Cell Fractionation / Q000379:methods; D002467:Cell Nucleus / Q000737:chemistry*; D002850:Chromatography, Gel / Q000379:methods; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000302:isolation & purification*; D002942:Circular Dichroism; D004229:Dithiothreitol; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification; D008297:Male; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013087:Spermatids / Q000737:chemistry*; D013552:Swine
D002868:Chromosomal Proteins, Non-Histone; C053886:spermatid transition proteins; D010450:Endopeptidases; D004229:Dithiothreitol