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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1988-7-1
|
| pubmed:abstractText |
Wheat embryo histone H3 has been isolated and purified and the elucidation of the complete amino-acid sequence is described. Peptides were generated by cleavages with CNBr, S. aureus V8 proteinase, endoproteinase Lys-C and trypsin. The peptides were purified by HPLC and the sequence determined by solid-state and gas-phase sequencing methodology. The amino-acid sequence of the protein is identical to pea embryo histone H3 and the sequence deduced from the nucleotide sequence of a wheat embryo histone gene (Tabata T. et al. (1984) Mol. Gen. Genet. 196, 397-400).
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0177-3593
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
369
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
193-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:3285855-Amino Acid Sequence,
pubmed-meshheading:3285855-Histones,
pubmed-meshheading:3285855-Indicators and Reagents,
pubmed-meshheading:3285855-Molecular Sequence Data,
pubmed-meshheading:3285855-Peptide Fragments,
pubmed-meshheading:3285855-Peptide Hydrolases,
pubmed-meshheading:3285855-Plants,
pubmed-meshheading:3285855-Triticum
|
| pubmed:year |
1988
|
| pubmed:articleTitle |
The primary structure of histone H3 from wheat.
|
| pubmed:affiliation |
UCT/CSIR Research Centre for Molecular Biology, Department of Biochemistry, University of Cape Town.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|