The two major protein components of bovine seminal plasma, PDC-109 and BSP I, have been purified by gel filtration, partition chromatography and reverse-phase high performance liquid chromatography from an 86% ethanol precipitate of bovine seminal plasma ejaculate. The complete 109-residue amino acid sequence of PDC-109 has been established by automated Edman degradation of the intact peptide as well as its proteolytic digestion and cyanogen bromide cleavage fragments. The 12,774 dalton structure has two structurally similar domains of 38 and 41 amino acids, each containing two disulfide bonds.
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| rdfs:comment |
The two major protein components of bovine seminal plasma, PDC-109 and BSP I, have been purified by gel filtration, partition chromatography and reverse-phase high performance liquid chromatography from an 86% ethanol precipitate of bovine seminal plasma ejaculate. The complete 109-residue amino acid sequence of PDC-109 has been established by automated Edman degradation of the intact peptide as well as its proteolytic digestion and cyanogen bromide cleavage fragments. The 12,774 dalton structure has two structurally similar domains of 38 and 41 amino acids, each containing two disulfide bonds.
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| skos:exactMatch | |
| uniprot:name |
Biochem. Biophys. Res. Commun.
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| uniprot:author |
Boehlen P.,
Esch F.S.,
Guillemin R.,
Ling N.C.,
Ying S.Y.
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| uniprot:date |
1983
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| uniprot:pages |
861-867
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| uniprot:title |
Primary structure of PDC-109, a major protein constituent of bovine seminal plasma.
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| uniprot:volume |
113
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| dc-term:identifier |
doi:10.1016/0006-291X(83)91078-1
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