The amino acid sequence of a boar transition protein 3.
The boar transition protein 3 (TP3) was extracted with acid from the isolated late spermatid nuclei or directly from the testes, fractionated with trichloroacetic acid, and reduced and carboxymethylated (RCM-). RCM-TP3 from the nuclei was purified by HPLCs on Nucleosil 300 7C18 and Hitachi #3057, and that from the testes, by ion-exchange chromatography on CM-Sephadex C-25 and HPLCs on Nucleosil 300 7C18 and Chemcosorb 7C8. The two TP3 preparations were identical in acid-urea- and SDS-gel electrophoretic mobilities and amino acid composition. The primary structure of TP3 was determined by manual Edman degradation of the peptides obtained by lysyl endopeptidase-digestion or by alpha-chymotrypsin-digestion of RCM-TP3 from the testes, and by automated Edman degradation of it. Boar TP3 is a basic protein of 76 residues: H-AKVTEKSWQPQTTSTKRWKKRKTPSQPRSRGKVRKIYKKVKRPLHVCSRKKYSPKVITTSRRQKRAR RANKFETIP-OH, and it shows 27% homology with boar TP1. TP3 is composed of an N-terminal region (1-19) having two characteristic tryptophan residues (8 and 18) which is absent in the known TP1 group, and a C-terminal region (20-76) having a close resemblance to boar TP1.
Akama
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Department of Chemistry, Faculty of Science, Chiba University.
Oka
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Tobita
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Hayashi
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D000595:Amino Acid Sequence; D000818:Animals; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000302:isolation & purification; D002918:Chymotrypsin; D008297:Male; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases; D013087:Spermatids / Q000737:chemistry*; D013552:Swine; D013737:Testis / Q000737:chemistry*
D002868:Chromosomal Proteins, Non-Histone; C053886:spermatid transition proteins; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C036813:lysyl endopeptidase