The antitumor action of seminal ribonuclease and its quaternary conformations
Authors:
- Claudia De LorenzoClaudia De Lorenzo
- Alberto Di DonatoADAlberto Di Donato
- Giuseppe D'ALessioGDGiuseppe D'ALessio
- 6 February 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 359 (1) , 31-34
Abstract
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.Keywords
This publication has 8 references indexed in Scilit:
- Ribonuclease A can be transformed into a dimeric ribonuclease with antitumor activityJournal of Biological Chemistry, 1994
- Expression of Bovine Seminal Ribonuclease in Escherichia coliBiochemical and Biophysical Research Communications, 1993
- New techniques for the determination of the scale and overall isotropic temperature factorsActa Crystallographica Section A Foundations of Crystallography, 1993
- New and cryptic biological messages from RNasesTrends in Cell Biology, 1993
- Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitorBiochemical Journal, 1992
- Seminal RNase: a unique member of the ribonuclease superfamilyTrends in Biochemical Sciences, 1991
- Secretion of Intact Proteins and Peptide Fragments by Lysosomal Pathways of Protein DegradationJournal of Biological Chemistry, 1989
- The effect of bovine seminal ribonuclease (AS RNase) on cells of crocker tumour in miceCellular and Molecular Life Sciences, 1973