The amino acid sequence and phosphorylation sites of a boar transition protein 1.
Boar transition protein 1 was extracted with acid from the testes, purified by chromatographies on CM-Sephadex C-25 and Sephadex G-50, and reduced and carboxymethylated. The modified protein was purified by HPLC on Nucleosil 300 7C18. The primary structure of the protein was determined by automated Edman degradation of the C-terminal peptide of the BrCN-cleaved protein and of the whole protein, and by carboxypeptidase digestion of it. The study of phosphorylation sites showed that Ser36 and Ser39 in the very conserved sequence 29-42 were partly phosphorylated, suggesting the involvement of this region in the interaction with DNA.
Akama
K
K
Department of Chemistry, Faculty of Science, Chiba University, Japan.
Kojima
S
S
Nakano
M
M
Tobita
T
T
Hayashi
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002852:Chromatography, Ion Exchange; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D010766:Phosphorylation; D013552:Swine; D013737:Testis / Q000737:chemistry
D002868:Chromosomal Proteins, Non-Histone; C053886:spermatid transition proteins