rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1993-10-12
|
pubmed:abstractText |
The DNA cleavage experiments show that C-1027 chromophore is selectively incorporated into C-1027 apoprotein and is strongly protected by the apoprotein from loss of its DNA cleaving activity. Fluorescence and circular dichroism spectra reveal (1) important participation of tertiary structure of C-1027 apoprotein for the chromophore binding, (2) specific 1:1 binding of C-1027 chromophore to the apoprotein, and (3) significant interaction of the benzoxazine group in the chromophore-apoprotein complex. On the other hand, C-1027 apoprotein does not contribute to sequence-specificity DNA cleavage by C-1027 antibiotics.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
195
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
659-66
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8373405-Aminoglycosides,
pubmed-meshheading:8373405-Anti-Bacterial Agents,
pubmed-meshheading:8373405-Antibiotics, Antineoplastic,
pubmed-meshheading:8373405-Apoproteins,
pubmed-meshheading:8373405-Circular Dichroism,
pubmed-meshheading:8373405-DNA,
pubmed-meshheading:8373405-Enediynes,
pubmed-meshheading:8373405-Models, Structural,
pubmed-meshheading:8373405-Protein Structure, Tertiary,
pubmed-meshheading:8373405-Proteins,
pubmed-meshheading:8373405-Spectrometry, Fluorescence
|
pubmed:year |
1993
|
pubmed:articleTitle |
Specific interaction between a novel enediyne chromophore and apoprotein in macromolecular antitumor antibiotic C-1027.
|
pubmed:affiliation |
Institute for Chemical Research, Kyoto University, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|