title: Full antitumor action of recombinant seminal ribonuclease depends on the removal of its N-terminal methionine.
abstract: 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.
authors.affiliation: Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Italy.
authors.forename: B S
authors.initials: BS
authors.lastname: Adinolfi
authors.forename: V
authors.initials: V
authors.lastname: Cafaro
authors.forename: G
authors.initials: G
authors.lastname: D'Alessio
authors.forename: A
authors.initials: A
authors.lastname: Di Donato
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D001483:Base Sequence; D002417:Cattle; D002470:Cell Survival / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008297:Male; D008715:Methionine / Q000737:chemistry*; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000494:pharmacology; D012260:Ribonucleases / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D012669:Seminal Vesicles / Q000201:enzymology*; D013329:Structure-Activity Relationship; D014407:Tumor Cells, Cultured
chemical_list: D000970:Antineoplastic Agents; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D008715:Methionine; D012260:Ribonucleases