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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1994-8-4
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1039-9712
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-57
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:8019440-Amino Acid Sequence,
pubmed-meshheading:8019440-Animals,
pubmed-meshheading:8019440-Binding Sites,
pubmed-meshheading:8019440-Chromatography, Ion Exchange,
pubmed-meshheading:8019440-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:8019440-Male,
pubmed-meshheading:8019440-Molecular Sequence Data,
pubmed-meshheading:8019440-Phosphorylation,
pubmed-meshheading:8019440-Swine,
pubmed-meshheading:8019440-Testis
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pubmed:year |
1994
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pubmed:articleTitle |
The amino acid sequence and phosphorylation sites of a boar transition protein 1.
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pubmed:affiliation |
Department of Chemistry, Faculty of Science, Chiba University, Japan.
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pubmed:publicationType |
Journal Article
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