Mancheño J M, Gasset M, Oñaderra M, Gavilanes J G, D'Alessio G
Departamento de Bioquímica y Biología Molecular, Facultad de Química, Universidad Complutense, Madrid, Spain.
Biochem Biophys Res Commun. 1994 Feb 28;199(1):119-24. doi: 10.1006/bbrc.1994.1202.
Bovine seminal ribonuclease (BS-RNase), an antitumor protein selectively cytotoxic for malignant cells, (i) specifically aggregates negatively charged vesicles and modifies the thermotropic behaviour of the phospholipid; (ii) decreases the amplitude of the thermal transition of the phospholipid; and (iii) provokes lipid-mixing between bilayers of negatively charged vesicles. This engenders leakage of the aqueous vesicle contents. Monomeric BS-RNase, devoid of antitumor action, does not produce these effects. These results suggest that the destabilization of the membrane bilayer promoted by BS-RNase may be involved in the antitumor action of the protein.