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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1989-3-23
|
| pubmed:abstractText |
A protein which preferentially binds Z-form duplex DNA has been purified from the cells of Deinococcus radiodurans. The molecular weight of the protein was estimated to be approximately 68,000 by gel filtration and SDS-polyacrylamide gel electrophoresis. Amino acid analysis of the protein indicates that it is not so basic since it contains a lower mole percent of lysine and higher mole percent of aspartic acid than those in histone-like DNA binding protein II (HU) of Escherichia coli. The first fifteen amino acid residues from the N-terminus have been also determined.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-924X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
104
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
127-30
|
| pubmed:dateRevised |
2007-12-19
|
| pubmed:meshHeading | |
| pubmed:year |
1988
|
| pubmed:articleTitle |
Isolation of a DNA-binding protein from Deinococcus radiodurans having an affinity for a Z-form polynucleotide.
|
| pubmed:affiliation |
Radiobiology Laboratory, Institute of Physical and Chemical Research, Saitama.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|