Source:http://linkedlifedata.com/resource/pubmed/id/17905622
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2007-12-14
|
pubmed:abstractText |
An extract of the skin of the Japanese tree frog, Hyla japonica Günther, 1859 (Anura: Hylidae) did not inhibit the growth of the bacteria Escherichia coli or Staphylococcus aureus, but contained a protein that was strongly hemolytic against human erythrocytes. The protein was purified to near homogeneity by reverse-phase HPLC, and its N-terminal amino acid sequence (SGRGKGGKGL...) identified it as histone H4. The complete primary structure of the 102-amino-acid-residue histone H4 was determined by a combination of molecular cloning of genomic and complementary DNAs encoding the protein. The molecular mass of the purified histone H4 determined by electrospray mass spectrometry was 71+/-2 Daltons greater than that predicted from the deduced amino acid sequence of the protein. The +71 mass units is consistent with the proposal that the protein isolated from the skin was post-translationally modified by addition of one acetyl and two methyl groups. The stem-loop structure at the 3' flanking region of the H. japonica histone H4 gene, which acts as a transcription termination signal, contained a nucleotide sequence (5'-GGCTCTCCTCAGAGCC-3') with unusual structural features not seen in other histone genes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1096-4959
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
149
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
120-5
|
pubmed:dateRevised |
2008-8-11
|
pubmed:meshHeading |
pubmed-meshheading:17905622-Amino Acid Sequence,
pubmed-meshheading:17905622-Amphibian Proteins,
pubmed-meshheading:17905622-Animals,
pubmed-meshheading:17905622-Anura,
pubmed-meshheading:17905622-Complex Mixtures,
pubmed-meshheading:17905622-Erythrocytes,
pubmed-meshheading:17905622-Escherichia coli,
pubmed-meshheading:17905622-Hemolysis,
pubmed-meshheading:17905622-Hemolytic Agents,
pubmed-meshheading:17905622-Histones,
pubmed-meshheading:17905622-Humans,
pubmed-meshheading:17905622-Molecular Sequence Data,
pubmed-meshheading:17905622-Protein Structure, Secondary,
pubmed-meshheading:17905622-Skin,
pubmed-meshheading:17905622-Staphylococcus aureus,
pubmed-meshheading:17905622-Transcription, Genetic
|
pubmed:year |
2008
|
pubmed:articleTitle |
Characterization of a hemolytic protein, identified as histone H4, from the skin of the Japanese tree frog Hyla japonica (Hylidae).
|
pubmed:affiliation |
Department of Biology, Faculty of Science, Toho University, Funabashi, Chiba 274-8510, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|