Isolation of intact transition protein 1 and 3 from boar late spermatid nuclei.
Boar transition protein 1 and 3 were extracted with acid from the late spermatid nuclei, separated from the TP-degrading proteases by ion-exchange chromatography on Fractogel EMD SO3- 650 (M), and further purified by HPLCs on Diol-120 and on Hitachi #3057, respectively. The circular dichroic spectra of the transition proteins with and without dithiothreitol showed that they have beta-form predominantly. Although sodium dodecyl sulfate partially induced helical structure, the beta-form was considerably retained. These indicate that the transition proteins have a structure-forming potential for the beta-structure.
Akama
K
K
Department of Chemistry, Faculty of Science, Chiba University, Japan.
Kosuge
M
M
Sato
H
H
Yamaoka
Y
Y
Nakano
M
M
Tobita
T
T
D000818:Animals; D002467:Cell Nucleus / Q000737:chemistry*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000302:isolation & purification; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D013087:Spermatids / Q000737:chemistry*; D013552:Swine
D002868:Chromosomal Proteins, Non-Histone; C053886:spermatid transition proteins