Statements in which the resource exists as a subject.
PredicateObject
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: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