Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-8-4
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
349-57
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The amino acid sequence and phosphorylation sites of a boar transition protein 1.
pubmed:affiliation
Department of Chemistry, Faculty of Science, Chiba University, Japan.
pubmed:publicationType
Journal Article