Biochemical and biophysical research communications, 1995-08, Vol.213 (2), p.525-532
1995
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Details
- Autor(en) / Beteiligte
- Titel
- Full Antitumor Action of Recombinant Seminal Ribonuclease Depends on the Removal of Its N-Terminal Methionine
- Ist Teil von
- Biochemical and biophysical research communications, 1995-08, Vol.213 (2), p.525-532
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 1995
- Quelle
- Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0006-291XeISSN: 1090-2104DOI: 10.1006/bbrc.1995.2163Titel-ID: cdi_crossref_primary_10_1006_bbrc_1995_2163
- Format
- –
- Schlagworte
- Amino Acid Sequence, Animals, Antineoplastic Agents - pharmacology, Base Sequence, Cattle, Cell Survival - drug effects, Hydrogen-Ion Concentration, Macromolecular Substances, Male, Methionine - chemistry, Mice, Molecular Sequence Data, Mutagenesis, Site-Directed, Polymerase Chain Reaction, Protein Conformation, Recombinant Proteins - chemistry, Recombinant Proteins - pharmacology, Ribonucleases - chemistry, Ribonucleases - genetics, Ribonucleases - pharmacology, Seminal Vesicles - enzymology, Structure-Activity Relationship, Tumor Cells, Cultured