|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1995-9-21
|
|
pubmed:abstractText |
Bovine seminal RNase (BS-RNase) is a dimeric member of the pancreatic-like ribonuclease superfamily, with antitumor activity. We report here that recombinant Met(-1) BS-RNase is a less potent cytotoxic factor, while structurally and catalytically indistinguishable from BS-RNase isolated from natural sources. Mature recombinant BS-RNase instead displays full antitumor action. This suggests that the conformation of the N-terminal region of BS-RNase is among the structural determinants of its antitumor action, in addition to its catalytic activity and its quaternary structure.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0006-291X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
213
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
525-32
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:7646508-Amino Acid Sequence,
pubmed-meshheading:7646508-Animals,
pubmed-meshheading:7646508-Antineoplastic Agents,
pubmed-meshheading:7646508-Base Sequence,
pubmed-meshheading:7646508-Cattle,
pubmed-meshheading:7646508-Cell Survival,
pubmed-meshheading:7646508-Hydrogen-Ion Concentration,
pubmed-meshheading:7646508-Macromolecular Substances,
pubmed-meshheading:7646508-Male,
pubmed-meshheading:7646508-Methionine,
pubmed-meshheading:7646508-Mice,
pubmed-meshheading:7646508-Molecular Sequence Data,
pubmed-meshheading:7646508-Mutagenesis, Site-Directed,
pubmed-meshheading:7646508-Polymerase Chain Reaction,
pubmed-meshheading:7646508-Protein Conformation,
pubmed-meshheading:7646508-Recombinant Proteins,
pubmed-meshheading:7646508-Ribonucleases,
pubmed-meshheading:7646508-Seminal Vesicles,
pubmed-meshheading:7646508-Structure-Activity Relationship,
pubmed-meshheading:7646508-Tumor Cells, Cultured
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Full antitumor action of recombinant seminal ribonuclease depends on the removal of its N-terminal methionine.
|
|
pubmed:affiliation |
Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
