The antitumor action of seminal ribonuclease and its quaternary conformations.
It has been previously shown that the antitumor action of bovine seminal ribonuclease (BS-RNase) is dependent on its dimeric structure. However, two distinct quaternary structures, each in equilibrium with the other, have been described for the enzyme: one in which the two subunits exchange their N-terminal ends, the other with no exchange. Antitumor activity assays, carried out on homogeneous quaternary forms of the enzyme, as well as on dimeric mutants of bovine pancreatic RNase A, reveal that another structural determinant of the antitumor activity of BS-RNase is the exchange of N-terminal ends between subunits.
Dipartimento di Chimica Organica e Biologica, Università Federico II di Napoli, Italy.
V
V
Cafaro
C
C
De Lorenzo
R
R
Piccoli
A
A
Bracale
M R
MR
Mastronicola
A
A
Di Donato
G
G
D'Alessio
D016475:3T3 Cells; D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D002417:Cattle; D002470:Cell Survival / Q000187:drug effects; D046911:Macromolecular Substances; D008297:Male; D051379:Mice; D016297:Mutagenesis, Site-Directed; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D012260:Ribonucleases / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D012661:Semen / Q000201:enzymology*; D013329:Structure-Activity Relationship; D014407:Tumor Cells, Cultured
D000970:Antineoplastic Agents; D046911:Macromolecular Substances; D012260:Ribonucleases